诗经，卫风

投我以木瓜，报之以琼琚。匪报也，永以为好也。
投我以木桃，报之以琼瑶。匪报也，永以为好也。
投我以木李，报之以琼玖。匪报也，永以为好也。

Here is where the sun rise

Here is where the sun rise

在废墟与虚构的边缘（10）

信人: junction (楼高不见章台路), 信区: Campus_Digest
标 题: 在废墟与虚构的边缘（10）
发信站: 日月光华 (2004年03月16日19:02:43 星期二), 站内信件

10. 暗藏

我需要接受某种暗示 /那些不被感知的
/始终存在。在墙角 /它们偷偷的唱歌……

我觉得自己响亮地高歌起来，带着欢快的样子，却困难得发不出声音，而且无法动弹。此后，我被尖叫惊醒，那是发自于我干涩喉咙的尾音，几行文本拖着余韵徐徐消逝。被子的边缘，搭在喉结上了，这是糟糕的意外。我先把还能记住的句子摘录下来，目的是为了向隐匿于省略号之后光环表示敬意。然后，用手腕抵了抵被角，便迫不及待地继续睡去。

在随后的睡眠中，我经历了惊悸，盗汗，并且不停痉挛的过程。那里充满油画色彩，遍布古希腊所崇尚的气质，健壮，厚实，然而神经质般地扭曲着。那里也有天使，不断给予我详和的抚慰，听起来却是一惊一咋的，唠叨不休。我看得见一片大草地，弯弓一样的天空，下面隆起一幢幢肥嘟嘟的房屋。我回到童年去了，掉入乳白色的被单里了。棉花下面，有着暗藏的一切。


--
这里的空气像玛瑙色糨糊。
※ 来源:·日月光华 bbs.fudan.edu.cn·[FROM: 10.45.10.103]

在废墟与虚构的边缘（9）

发信人: junction (楼高不见章台路), 信区: Campus_Digest
标 题: 在废墟与虚构的边缘（9）
发信站: 日月光华 (2004年03月16日18:59:32 星期二), 站内信件

9. 重心

有时我沿着布朗运动的思路，对瞬间作出如下设想：世界上大体每个人都是沿着某条线段行动的，线是某条曲线的瞬时切线，指引着行动的方向。无论这方向怎样缩短了或拉长了岁月，它都是牵扯着零乱的足迹以及连贯的足迹走向一个中心。在中心人不会寂寞，人可以心平气和的最后老死在那里，无所谓遗憾，安然瞑目。为此，人们寻找着圆以及它中间沉甸甸的那点。

行走在直径上的人是有福的，而在弦或圆周切线上漫步的人只好接受暂时漂泊的命运，跟某种事物擦肩而过，继而越离越远。

在“坐着”那首诗里，我曾写道：我担心一辈子狂奔/也追不上别人离我远去的速度。记得写到这两行时，我很煽情的泪流满面。这是没有人知道的，他们也不知道我对于中心的渴望。没长眼睛的线段总是自顾自从一座城市搭往另一座城市，使我一度精神上忘记了家乡，我的父母，活过三个朝代的爷爷，和在那一年去世的奶奶。坐在床头，我平放的手巍然没动，仿佛坐在池塘上空，那水面似乎冻住了。

这么想的时候，房间里头常常是漆黑的，意味着夜幕已经降临了很久。我必需睁大眼睛在黑暗中适应一段时间，才能些许看清一些梦幻的实质。好比达芬奇在他老师的画布上描下的那个天使，身边是他木讷的伙伴，以及愤怒而略现暴戾的施洗者约翰，还有枯瘦的受洗者耶稣。可现在，我需要闭上眼睛了，该停止思路的时候了。夜深了，不如睡吧。

阳台呼呼着响，隔着玻璃门跟我的心脏产生共振，使它疲惫而不致于衰竭。我明白，那里的灰很重了罢，总是有一些泥土会被风吹走，有一些沉淀下来。没有办法。

人生像一场叙事，在咶噪的絮絮叨叨中突然会失去论述的方向。如同我的思维，刚才激动莫名，一会儿就苍白如洗了。在弦和切线上，这冥冥通往中心的幻觉里，接受背离的命运。在房间里，我不停地改变行动姿势，仿佛支持不稳的样子忐忑不宁，无非是坐着，躺着，偶尔站立起来。毫无疑问，下一个时刻，线段的端点就会到来，它将带着抚慰似的迎风而至。可我，也许不得不以此踏上陌生，归宿于逃逸，或者漂泊。身不由己地寻找那日渐失真的圆周，并试图探测它的重心。



--
这里的空气像玛瑙色糨糊。
※ 来源:·日月光华 bbs.fudan.edu.cn·[FROM: 10.45.10.103]

在废墟与虚构的边缘（8）

发信人: junction (叹息的两端), 信区: Campus_Digest
标 题: 在废墟与虚构的边缘（8）
发信站: 日月光华 (2003年07月16日15:30:09 星期三), 站内信件

8. 悖论

有时候，我会在肥皂泡哔哔啵啵的声响中悄然醒来。光线和颜色同以往一样，分别占据着白与黑的两端。仿佛有数不清的方框，数不清的圆圈正从眼前一环环荡漾开去，在空洞的大气中，尘粒和水滴的缝隙之间，勾勒出了无穷多个跟我存活着的世界相等价的世界。我无法说明这些世界是不存在的，就像我的心跳或者呼吸，有时表达着生命的迹象，有时却离我十分遥远，占据着一种异常不真实的姿势。我常常设想，在某个表象空间的坐标里，也许有一头牛正跟我叠处于同一个坐标，一如那挥之不去的岁月思绪，蒙满了这个房间，充塞了皮肤以内的真实世界。当我沉浸在这些不可证伪的世界里，聆听着哔哔啵啵的声音，随后便会沉沉地重新睡去。

偶尔，雨不知道是什么时候下起来的，我似乎闻到了黄浦江边潮湿的腥味。我想象如果布满鞋印的地面没有人影，那将是什么样的景色？一向喧嚣的外滩也许会跟稀疏的雨滴一样零零落落。宽厚的水泥护栏与花圃边沿呈直角相交，我和Y 在顶点处分别占据一边，作为孤独的单元，我们屈膝而坐，面对面中间隔着一瓶矿泉水。我们的气息在矿泉水周围形成驻波，波节和波腹都是我们痴迷的逻辑陷阱。

比如，如果一开始是方框进入我的眼帘，历经我的大脑并从我嘴里说出方框；然后方框传进Y的耳朵，解析之后结果为圆圈，历经Y的大脑并从Y 的嘴里说出圆圈；然后圆圈传进我的耳朵，解析之后结果为方框，方框反馈至我的大脑完毕。于是，我对这样的交流表示满意。反之亦然，Y 因此把我当作知音。在我们的宿命里头，我们不知道我们到底是拥有共同的方框，或者共同的圆圈，或者连接方框与圆圈的一个悖论。

悖论意味着一种殇，等同于一幅忧伤的图画。如果我们是在一个和谐的悖论中美美睡着了，也许上帝也不会愿意使我们苏醒。于是，当驻波成型，肥皂泡将继续哔哔啵啵响着，哔哔啵啵的世界里，我们拥有了共同的方框，或者圆圈。


--
深渊两边，时间的悬崖，我依靠眼前面孔的变化完成移动。
※ 来源:·日月光华 bbs.fudan.edu.cn·[FROM: 10.45.10.133]

在废墟与虚构的边缘（7）

发信人: junction (叹息的两端), 信区: Campus_Digest
标 题: 在废墟与虚构的边缘（7）
发信站: 日月光华 (2003年05月27日18:35:02 星期二), 站内信件

7. 礼物

几年前，因为学业我在一个古代被称作明州的地方蛰居。一个漫长的雨季使我得了抑郁症，梅雨使那里的三条江趁机泛滥了，让人有鼻子发酸的理由。我在狭窄的宿舍里等到了天高气爽的秋天，阳光的来临使我的抑郁症愈发变得沉重。终于有一天，天气十分明媚，我抱了一大络纸，躲在洗手间水池边的角落里，用一个洋瓷脸盆把它们烧掉了。那天我还写了这辈子最得意的一首长长的古风，当然，古风也在那个洋瓷脸盆里化掉了。许多年以后的今天，我只记得古风开头的四句：
天开云昕时正瑞，雁声缭绕教魂催。
青烟淡散随魂逝，伴愁生死复一回。
而别的许多东西就这么消失了。我虽然滥情，却无法承受它们一辈子，尽管它们也许还会在我的脑海里久久地盘踞一点。

我不知道这辈子遇上的哪些东西是命运作为礼物送给我的。刚开始我总是一厢情愿地收集它们，然后它们似乎就真的跟我息息相关了。我必须尽可能地把它们全部带在身边，因为我无法把任何微小的它遗留在某个孤独的角落，以至使我的灵魂会因为它变得孤独——只有上帝知道我是多么不善于忍耐寂寞。用泰戈尔的话来说：即使一刻不看见，也是不行的。有时候这种话我也会脱口而出，那样子Y就会跟我相视一笑。

人生路上，我就像一个越滚越大的雪球，这雪球终有超出上帝赋予我的携带能力的时候，于是雪球碎开了。不管我乐不乐意，它们就自己离开我的视野，有时是我不得不把视线移开它们。这种事情在我的记忆里不止发生一次，事情由于被忘记或者遭受忽视所以一次一次重复。后来，我越来越不敢接收各种所谓的礼物了，虽然我依旧有所渴望。

说起来，Y其实比我还滥情，这点在她搬家的时候我才知道。但是，她自己没有明白这个。她的礼物几乎溢出了她的记忆空间，只是在整理的时候才一样一样还原，它们多多少少都已经进入她的生命，若不想残忍，是不能分开的。我的渴望得到了许多满足，是因为Y把许多东西寄放到我那里，有些东西已经散布于我的书架，如同那些贝壳。这些命运交付给我的东西现在也跟我息息相关了，如果把它们跟我分开，我想我们互相都会觉得寂寞。


--
深渊两边，时间的悬崖，我依靠眼前面孔的变化完成移动。
※ 来源:·日月光华 bbs.fudan.edu.cn·[FROM: 10.13.85.200]

在废墟与虚构的边缘（6）

发信人: junction (叹息的两端), 信区: Campus_Digest
标 题: 在废墟与虚构的边缘（6）
发信站: 日月光华 (2003年05月27日18:33:46 星期二), 站内信件

6. 行动

不自觉地置身于光环当中，几乎已经成为人的本能。在一小块空间里头，我自己也不知道我跟恪守这个行动有什么关系，放弃与逃离似乎早已被睿智扫荡掉了，唯有时间仍然执拗地拉着我往某个终点奔向。老实说，我选择坐着并不是因为我有先见的智慧，只不过我逃来逃去最终还是这么个样子，到最后才向徒劳缴械并报以微笑的。我就这样子被禁闭了。

每当夜晚来临的时候，我能感受到许许多多的眼光，它们都来自记忆中的某段时空。这些眼光有时在空气中编织成茧，有时像一条条飞舞着的鞭子，向我暗示着观测、探询等一系列动词，它们起源于自外而内的光线。对我来说，内和外隔着一堵厚墙，这个被阻塞的唯一通道并不是可逆的，当那些外来的光线被皮肤阻挡之后，探询也就变得没有多少意义了。然而，我也没有想象的那么坦荡，在光线的照耀下有时会有蚂蚁从记忆的河谷中爬出来，偷偷地咬我一口，我的神经颤栗了，我就会啊的大叫起来。


--
深渊两边，时间的悬崖，我依靠眼前面孔的变化完成移动。
※ 来源:·日月光华 bbs.fudan.edu.cn·[FROM: 10.13.85.200]

在废墟与虚构的边缘（5）

发信人: junction (叹息的两端), 信区: Campus_Digest
标 题: 在废墟与虚构的边缘（5）
发信站: 日月光华 (2003年05月16日14:20:08 星期五), 站内信件

5. 贝壳

—— 一千件无聊的事天天在发生
为什么这样一件事不能够偶然实现
泰戈尔

许多我意料之外的事发生了，许多我意料之外的事一直没有发生，而那些属于我意料之中的常常被我忘却。当上帝不停地拨弄我的肩膀的时候，它们就像没有来处的惊喜，只是稍微让我感知一下就轻擦着大脑皮层拐走了。从来的地方来，到去的地方去。不是因为有什么理由，现在，我把视线移至书架，抚摸着那些散放在书架上的贝壳。关于贝壳的来历，还的从J讲起。

我认识的J是一个粗胚，本来这个偏见是不会改变的。有人告诉我，J两只眼睛的外角耷拉着下垂，这是一付天然的满含悲伤的面相。那之后，当我继续回想起这个长着络腮胡子的家伙时不时像小女生一样啜泣样子，也就觉得平常并且能够接受了。

贝壳跟我的同学J有某种不易被察觉也不易被忽略的关系，这点是我的女友Y后来不经意时提醒我的。贝壳之间立着五个精致小巧的稻草人，它们右边的衣橱壁上贴着两个很漂亮小挂钩，挂钩钩着两个一样大小的中国结。我的视线牵扯着，轻轻地拨弄着，明白房间的某个角落里，还有一罐跟秋天的树叶放一块的幸运星。我不能不感到一种激动和慰籍，但我却因此忘记了许多应该记住的细节。当我在未来的岁月突然发现完美中间有一块斑点的时候，宿命所带来的缺憾已经无法改变了。

记得中学时候的我从自卑走向狂妄，大学时候的我坚信自己已经到了上帝的身边，由于深刻而变得幼稚。J就是我幼稚年代里认识的同班同学，还是同宿舍的室友。我对J的认可，把他当作非常熟悉的人，以至可以相互玩一些思维上的把戏，在一些时间的端上可以用拥抱来表达重逢的喜悦，就是说我们成为人们所说的哥儿们了，这个认可的拐点来得非常缓慢。从陌生到认识，从陌陌生生的认识到熟悉的认可，我往往需要非常长的时间，但看起来似乎只需短暂的一瞬。这点我跟我的女友Y是完全想同的。我
们跨越漫长的岁月从耳闻走到陌生从陌生走到认识从认识走到熟悉从熟悉走到单恋，然后她对我说对于一些事情的想象并不只是我单方面的，于是我们走到了相恋。

在这个冗长过程中，存在一个拐点，我突然因为幼稚而变成一个思维分析者。曾经，Y是一个用作掩饰并被我赋予复杂含义的字母，它现在是从另一个名字的拼音上摘下来的。我说我的女友，我是说一个患逻辑病的思维分析者从“多余人”变成了当事的主角。于是，当我跟我的女友Y站在一块，看着我的同学J满含伤痛并且固执地走进记忆，我们都觉得十分肃穆。我建议Y不妨哭一下，她摇摇头把一个神情永久地刻进了我的视网膜。我们从轻飘飘的无可奈何转向甜美地面对沉重，我们从被连根拔起重得落回地面，我们一下子仿佛有点儿不习惯了。书架上的贝壳安安静静地躺着。

我没想到事先会有一天，就像无意中安排好的一样，上帝写下了一个伏笔。那时候我说我还跟风一样自由，一样失魂落魄。我说我没有历史，我的历史跟我的日记一起被偷了，它们带上我的旅行包偷偷地自己出门观光去了。说着，我仿佛对一九九九年投去了眺望式的一瞥。其实，一九九九年之后，我的历史从苍白处又迅速膨胀了。当我意识到这点，短暂的过去已经变得无比沉重，我的前身终于捱过了他的晚年，打算安息了。上帝写下了一个单词，让它高频率晃入我的视野，等待做伏笔的那天。那个单词就是我的今身。不久之后，我和Y相恋了。一次偶然的机会我想起我的今身，今身的第一个字母J使我对万能的造物主报以无比崇高的敬畏。别的事情我已经不敢多想了。包括贝壳的来历，它们是我的同学J从普陀带回来的。我不敢多想了，我的今身就像这些曾经湿透的贝壳。

Y说那些贝壳你是不是洗过了。我说没有。她说它们本来是腥味很重的，现在自己蒸发掉了。J走进了记忆，这些贝壳是他留给我的，哦，不，是他丢下的，被我一厢情愿捡起来了。现在，我已经无法舍弃这些尽管逐渐亡但是确实将变作记忆的东西。这点情怀我的女友Y跟我十分相似。也许，将来会有一天，因为相似，我们将碰撞得一塌糊涂。我们化作灰烬，像凤凰一样涅槃。


--
深渊两边，时间的悬崖，我依靠眼前面孔的变化完成移动。
※ 来源:·日月光华 bbs.fudan.edu.cn·[FROM: 10.13.85.200]

在废墟与虚构的边缘(4)

发信人: junction (叹息的两端), 信区: Campus_Digest
标 题: 在废墟与虚构的边缘(4)
发信站: 日月光华 (2003年05月07日14:42:46 星期三)

4. 镜子

在镜子里头，我常常能够看见一个来回走动的身影，这是一个在单恋通往失恋路上徘徊不休的人。当然，我不想这么作出定论，因为他说他是一个徒步行往天堂的人，像一只蚂蚁爬进了水滴围成的沙漠。他说他爬上殿堂的尖顶，又回到地面，脚踩过的地方时空
开始扭曲，没有不可以发生的荒诞不可以延续的逻辑。他说单单拥有完美思想的上帝所处的困境跟任何一个俗人是一致而且同等的。他有一搭没一搭地叙述，他总是失去表情，呆呆地和我对视，呢喃着含混不清的话。我完全明白他的意思，这是不用置疑的，只有我知道他的心情是多么苍白，以及多么复杂。对于他来说，有些字眼是十分奢侈的，我不能轻易对他提起。事实上，我也无话可说，相同心境的人处在一起，自然而然会回避一些话题。也许在不确定的将来，就像我曾经在一首诗里写的那样：

我依然能够听见
我的空落落的脚步
依然无边无际地走着

等我很累的时候，我想我会停下来休息的。那样，我会看见镜子里头仿佛有了我自己的笑容。我将万分快慰地想起，我的心情跟上帝一样愉悦。


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深渊两边，时间的悬崖，我依靠眼前面孔的变化完成移动。

※ 来源:·日月光华 bbs.fudan.edu.cn·HTTP [FROM: 10.13.85.200]

在废墟与虚构的边缘(3)

发信人: junction (叹息的两端), 信区: Campus_Digest
标 题: 在废墟与虚构的边缘(3)
发信站: 日月光华 (2003年05月07日14:41:34 星期三)

3. 被子
被子如同座垫。记忆当中，一个人如果经常分不清虚拟的和所谓真实的，并且偶尔从时间的轴上摘取下一点，以此观望过去与未来两大深渊，我想这是符合上帝意旨的一种存在方式。我眷恋于某种毫无意义的废墟大背景，站在废墟与虚构的边缘，也许我会时常无意识地自言自语，梦呓一般嘀咕：啊，浪漫主义将要换个角度复苏了。我的眼角似乎就会一阵潮湿，接着毛孔一阵混乱，然后就觉得脸部涂上了一层钢蓝的颜色。把某种内涵重新包裹起来，装进已经被多次反复地弄皱烫平的皮肤里面。事实上，几十年的岁月过去了，我对于什么叫做浪漫主义其实一无所知，一点点也不知道。这个房间里头，我的被子像座垫一样。

我枯坐那里，时刻承受着大和小的双重折磨。在无助与充满渴望的情况下，面对着方式跟价值意识发生了矛盾。它们有时碰撞得一塌糊涂。

有一年，当夏天即将结束的时候，我简直要认为：“即使上帝与我同在，我也什么都不是了。”到了秋末，我和我的长长的身影一同走进一个看不见四壁的深谷。在那里面，我眼睁睁看着时间流逝，以及生命、价值、意义等各种信念的慢慢枯萎。我想起我的被子，它像座垫一样，供我盘腿栖息。于是，时间往往从夜晚23点缓缓划到了临晨2、3点钟。那些个空空落落的时刻，我偶尔设想着在没有祈祷的情况下，上帝将给予我的关注与仁慈。有时候，会有许许多多半真半假的形象，随同道听途说得来的各种价值标准，像幻灯片一样从我眼前晃过。于是，似乎就有悒郁的东西在每个细胞每个毛孔的角落里积累膨胀。每隔一小段时间，我必须设法把那些沉积的东西用某种方式释放，否则生命似乎难以为继了。这也就是我试图挣扎中能够做出的唯一努力。我觉得我就这么在细节里备受煎熬。一些刚开始行之有效的调味品，一旦对它寄以厚望，后来总是成为负担。正因为这些徒劳的挣扎，时间又一次把我抛下了很远的一段距离。

那些岁月里我的状态非常糟糕。我一直都在努力，甚至试图往每个毛孔里灌注能量，但我的心境跟时间一样，总是偷偷地就自己变了。生存的模式像水一样既不可预测又似乎清晰可见，有种让我无可适从的空洞。模模糊糊的意识当中，我仿佛觉得人生除了理性的追求之外，还有许多捉摸不透的其它细节同样令人不能轻易达到释怀。需要说明的是，这些细节不仅仅是人们传说中的感情。比如我那座垫一样的被子，当它轻轻地承受着我盘坐时的重量的时候，我就迷茫的久久不能释怀。

在一些非常突兀的瞬间，肥皂泡从四周涌起，迅速填满了皮肤之外的所有缝隙，直抵宇宙边缘。把我的躯体放倒，让我悬空平躺。肥皂泡哔哔啵啵的产生和湮灭的声音传递着来自边缘的信息，告诉我即使一口气睡过几百年也没有关系，我听不见大地上其他生物行走的声音，听不见猫头鹰惊动我童年时的召唤。肥皂泡哔哔啵啵响着，哔哔啵啵的有时突然无比巨大，有时迅速彤缩突然小得可以忽略不计。这种时候，我的被子似乎离我很远，很远。


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深渊两边，时间的悬崖，我依靠眼前面孔的变化完成移动。

※ 来源:·日月光华 bbs.fudan.edu.cn·HTTP [FROM: 10.13.85.200]

在废墟与虚构的边缘(2)

发信人: junction (叹息的两端), 信区: Campus_Digest
标 题: 在废墟与虚构的边缘(2)
发信站: 日月光华 (2003年04月21日20:39:24 星期一), 站内信件

2. 阳台

只有当现实走进了属于记忆的那方空间，我的生活才能够得以继续。我的故事跟我的人生一样，从来都是以半死不活的方式进行的，随时都可能中止，随时可能变回到事情还没开始的以前，或者直接跳到什么都还没有发生的以后。我无法相信比我的情绪更容易偷偷变化的时间。在以一种近乎静止的速度更替运动当中，我时常会想起阳台，那里的阳光、夜色，以及各种变幻莫测的星象都在我的血液里恬恬流动。我设想一些阳光明媚的午后，我慵倦地站在那里，观看一个人永远察觉不到有什么起伏的人间景色。我想这些都是我作为一个具有生物特征的人的写照。

然而，有一段子，我觉得自己快要活不下去了。那时候时间的转盘即将转过去四分之一个圆周，夏天快要到了，可冬天还在春天的地盘上肆虐横行，久不久弄得一团糟。但这团充满活力的糟糕终究也要慢慢沉淀的，慢慢下坠，然后变成凝固的样子。我想等到那候心跳可能已经是多余的事了，起伏将被淡忘。就像我的阳台，事实上那是一个布满灰尘的地方。我几乎不去那里了，也许非常细心的人还能够从逐渐变深的尘埃里头，看到我曾经在上面踩过的痕迹。通往阳台的那扇玻璃门把我的年龄分割成互相眺望的两段，很长一段时间里，我坐在房间里头，生命就在这种藕断丝连的对峙状态下慢慢消逝。直到有一天，我觉得再也没有什么力气了，便在玻璃上贴了一张白纸，把它们彻底分开。那种样子，一直保留至今。

我想我的阳台早就暗示了，有一天我将成为一个逻辑病患者。而在这之前充满沉默的岁月里，我已经锻炼得习惯于一个人的思维分析了。我甚至觉得心理医生这个名词，跟我有某种说不清楚的宿命相连，尽管我从来没有见过从事这种职业的人，他们跟我素昧平生。许多东西，可能我是永远无法逃脱的。就像我的人生，虽然习惯于正常了，却常常对某种起伏充满憧憬和眷念。这些都是我无法逃脱的。


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深渊两边，时间的悬崖，我依靠眼前面孔的变化完成移动。
※ 来源:·日月光华 bbs.fudan.edu.cn·[FROM: 10.13.85.200]

在废墟与虚构的边缘(引子)

发信人: junction (叹息的两端), 信区: Campus_Digest
标 题: 在废墟与虚构的边缘(引子)
发信站: 日月光华 (2003年04月20日20:29:28 星期天), 站内信件

1. 引子

我走出居民楼正是人们所说万家灯火的时分。五角场的车流像夜色下从容蠕动的一条蚯蚓，从翔鹰路一端爬来，绕过大圆盘，伸到邯郸路之后就被高楼挡住视线了。我决定步行回学校，接下来就跟人群擦肩，在蚯蚓被截断的地方横穿马路。一些不经意的时刻，我时不时地停下来站立一会，不关注任何东西，包括左右的人流和一对站在我右侧百货大楼下相拥而吻的长发男女。这是一个有很多人的风口，一种迷茫的东西在眼前的夜色里弥漫。很久之后，当我回想起那次经过五角场的情景，我完全陷入了一个人的皮肤里面那里是我最真实的空间。我还能清晰地感到我的头顶不停地擦着马路边的树叶，然后似乎就会有音乐响起。这些不可捉摸的忧伤旋律，一直充塞了我剩余人生的漫长岁月。

这都是一些奇怪的感觉。我记得那天回到实验室之后，便迫不及待地打开了winamp。当天晚上，空明跌宕音乐一直响彻至深夜，挤得一些东西从我的脑细胞里扑扑簌簌掉了出来，涂满我的面颊。

多年以后的今天，我正在听这首歌，同样的旋律，依然具有催人泪下忧伤魅力。所不同的是，经过岁月的过滤之后，我脸上如今显示的是一副不动声色的凝重——人是一种习惯正常的生物。正是这样的心态下，我写下了一个打算用文字来充实的标题：在废墟与虚构的边缘。


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深渊两边，时间的悬崖，我依靠眼前面孔的变化完成移动

Eph Receptors: a Paradoxical Family of Kinases

The Eph (erythropoietin-producing hepatocellular carcinoma) receptors

Rhodopsin

RACGAP1

Rac GTPase activating protein 1

棉袍

棉袍

灯芯绒长衬衫

Europium

铕是一种金属元素，银白色，能燃烧成氧化物；氧化物近似白色。铕熔点822°C，沸点1597°C，密度5.2434g/㎝³；是稀土元素中密度最小、最软和最易挥发的元素。铕为稀土元素中最活泼的金属：室温下，铕在空气中立即失去金属光泽，很快被氧化成粉末；与冷水剧烈反应生成氢气；铕能与硼、碳、硫、磷、氢、氮等反应。铕广泛用于制造反应堆控制材料和中子防护材料。用作彩色电视机的荧光粉，在铕(Eu)激光材料及原子能工业中有重要的应用。Europium原意是欧洲，1896年由法国化学家德马尔盖发现。

A Star in the Big Dipper Is an Alien Invader

吠月的犬

载着吠月的犬的列车滑过去消失了。
铁道叹一口气。
于是骑在多刺的巨型仙人掌上的全裸的少女们
的有个性的歌声四起了：
不一致的意义，
非协和之音。
仙人掌的阴影舒适地躺在原野上。
原野是一块浮着的圆板哪。
跌下去的列车不再从弧形地平线爬上来了。
但击打了镀镍的月亮的凄厉的犬吠却又被弹
回来，
吞噬了少女们的歌。

by 纪弦 1942年

一匹马看见我

一匹马看见我
我经过它的眼睛
走向大路

一匹马看见离奇的动物
她的手臂悬在空中
头顶上没有耳朵

我没有机会和一匹马
长久地呆在一起

by 巫昂

最后的情歌

我最终归属于这离奇的暖冬
屋内到屋外有一条蛇那么远
松鼠在叫门
一匹马带它走出森林
另一匹带你回来

by 巫昂

fight-or-flight response

Violet

Calendula

Lemon

The Cys-loop ligand-gated ion channel superfamily

The Cys-loop ligand-gated ion channel superfamily is composed of nicotinic acetylcholine, GABAA, GABAA-ρ, glycine, 5-HT3, and zinc-activated (ZAC) receptors. These receptors are composed of five protein subunits which form a pentameric arrangement around a central pore. There are usually 2 alpha subunits and 3 other beta, gamma, or delta subunits (some consist of 5 alpha subunits). The name of the family refers to a characteristic loop formed by 13 highly conserved amino acids between two cysteine (Cys) residues, which form a disulfide bond near the N-terminal extracellular domain.

Cys-loop receptors are known only in eukaryotes, but are part of a larger family of pentameric ligand-gated ion channels. Only the Cys-loop clade includes the pair of bridging cysteine residues.[1] The larger superfamily includes bacterial (e.g. GLIC) as well as non-Cys-loop eukaryotic receptors, and is referred to as "pentameric ligand-gated ion channels", or "Pro-loop receptors".[2]

All subunits consist of a large conserved extracellular N-terminal domain, three highly conserved transmembrane domains, a cytoplasmic loop of variable size and amino acid sequence, and a fourth transmembrane region with a relatively short and variable extracellular C-terminal domain. Neurotransmitters bind at the interface between subunits in the extracellular domain.

Each subunit contains four membrane-spanning alpha helices (M1, M2, M3, M4). The pore is formed primarily by the M2 helices.[3] The M3-M4 linker is the intracellular domain that binds the cytoskeleton.

5-HT3 receptor

The 5-HT3 receptor belongs to the Cys-loop superfamily of ligand-gated ion channels (LGICs) and therefore differs structurally and functionally from all other 5-HT receptors (5-hydroxytryptamine, or serotonin) receptors which are G protein-coupled receptors.[1][2][3] This ion channel is cation-selective and mediates neuronal depolarization and excitation within the central and peripheral nervous systems.[1]

As with other ligand gated ion channels, the 5-HT3 receptor consists of five subunits arranged around a central ion conducting pore, which is permeable to sodium (Na), potassium (K), and calcium (Ca) ions. Binding of the neurotransmitter 5-hydroxytryptamine (serotonin) to the 5-HT3 receptor opens the channel, which, in turn, leads to an excitatory response in neurons. The rapidly activating, desensitizing, inward current is predominantly carried by sodium and potassium ions.[2] 5-HT3 receptors have a negligible permeability to anions.[1] They are most closely related by homology to the nicotinic acetylcholine receptor.

5-HT Receptor - an overview

5-HT receptors, 5-hydroxytryptamine receptors , or serotonin receptors, are a group of G protein-coupled receptor and ligand-gated ion channels found in the central and peripheral nervous systems.[1][2][3] They mediate both excitatory and inhibitory neurotransmission. The serotonin receptors are activated by the neurotransmitter serotonin, which acts as their natural ligand.

The serotonin receptors modulate the release of many neurotransmitters, including glutamate, GABA, dopamine, epinephrine / norepinephrine, and acetylcholine, as well as many hormones, including oxytocin, prolactin, vasopressin, cortisol, corticotropin, and substance P, among others. The serotonin receptors influence various biological and neurological processes such as aggression, anxiety, appetite, cognition, learning, memory, mood, nausea, sleep, and thermoregulation. The serotonin receptors are the target of a variety of pharmaceutical and recreational drugs, including many antidepressants, antipsychotics, anorectics, antiemetics, gastroprokinetic agents, antimigraine agents, hallucinogens, and entactogens.[4]

Serotonin receptors are found in almost all animals and are even known to regulate longevity and behavioral aging in the primitive nematode, Caenorhabditis elegans.

Dystrophin

Dystrophin is a rod-shaped cytoplasmic protein, and a vital part of a protein complex that connects the cytoskeleton of a muscle fiber to the surrounding extracellular matrix through the cell membrane. This complex is variously known as the costamere or the dystrophin-associated protein complex (DAPC). Many muscle proteins, such as α-dystrobrevin, syncoilin, synemin, sarcoglycan, dystroglycan, and sarcospan, colocalize with dystrophin at the costamere.

The DMD gene, encoding the dystrophin protein, is one of the longest human genes known, covering 2.3 megabases (0.08% of the human genome) at locus Xp21. The primary transcript in muscle measures about 2,100 kilobases and takes 16 hours to transcribe;[5] the mature mRNA measures 14.0 kilobases.[6] The 79-exon muscle transcript[7] codes for a protein of 3685 amino acid residues.

DAG1

Dystroglycan is a protein that in humans is encoded by the DAG1 gene.[5][6][7]

Dystroglycan is one of the dystrophin-associated glycoproteins, which is encoded by a 5.5 kb transcript in Homo sapiens on chromosome 3.[8] There are two exons that are separated by a large intron. The spliced exons code for a protein product that is finally cleaved into two non-covalently associated subunits, [alpha] (N-terminal) and [beta] (C-terminal).

carnation oil painting

Transforming protein RhoA

Transforming protein RhoA, also known as Ras homolog family member A (RhoA), is a small GTPase protein in the Rho family of GTPases that in humans is encoded by the RHOA gene.[5] While the effects of RhoA activity are not all well known, it is primarily associated with cytoskeleton regulation, mostly actin stress fibers formation and actomyosin contractility. It acts upon several effectors. Among them, ROCK1 (Rho-associated, coiled-coil containing protein kinase 1) and DIAPH1 (Diaphanous Homologue 1, a.k.a. hDia1, homologue to mDia1 in mouse, diaphanous in Drosophila) are the best described. RhoA, and the other Rho GTPases, are part of a larger family of related proteins known as the Ras superfamily, a family of proteins involved in the regulation and timing of cell division. RhoA is one of the oldest Rho GTPases, with homologues present in the genomes since 1.5 billion years. As a consequence, RhoA is somehow involved in many cellular processes which emerged throughout evolution. RhoA specifically is regarded as a prominent regulatory factor in other functions such as the regulation of cytoskeletal dynamics, transcription, cell cycle progression and cell transformation.

Structure
The specific gene that encodes RhoA, RHOA, is located on chromosome 3 and consists of four exons,[6] which has also been linked as a possible risk factor for atherothrombolic stroke.

Similar to other GTPases, RhoA presents a Rho insert in its primary sequence in the GTPase domain. RhoA contains also four insertion or deletion sites with an extra helical subdomain; these sites are characteristic of many GTPases in the Rho family. Most importantly, RhoA contains two switch regions, Switch I and Switch II, whose conformational states are modified following the activation or inactivation of the protein. Both of these switches have characteristic folding, correspond to specific regions on the RhoA coil and are uniformly stabilized via hydrogen bonds. The conformations of the Switch domains are modified depending on the binding of either GDP or GTP to RhoA. The nature of the bound nucleotide and the ensuing conformational modification of the Switch domains dictates the ability of RhoA to bind or not with partner proteins (see below).

The primary protein sequences of members of the Rho family are mostly identical, with the N-terminal containing most of the protein coding for GTP binding and hydrolysis. The C-terminal of RhoA is modified via prenylation, anchoring the GTPase into membranes, which is essential for its role in cell growth and cytoskeleton organization. Key amino acids that are involved in the stabilization and regulation of GTP hydrolysis are conserved in RhoA as Gly14, Thr19, Phe30 and Gln63.

Correct localization of the RhoA proteins is heavily dependent on the C-terminus; during prenylation, the anchoring of the prenyl group is essential for the stability, inhibition of and the synthesis of enzymes and proliferation. RhoA is sequestered by dissociation inhibitors (RhoGDIs) which remove the protein from the membrane while preventing its further interaction with other downstream effectors.[7]

Activation mechanism
RhoA acquires both inactive GDP-bound and active GTP-bound conformational states; these states alternate between the active and inactive states via the exchange of GDP to GTP (conducted simultaneously via guanine nucleotide exchange factors and GTPase activating factor). RhoA is activated primarily by guanine nucleotide exchange factors (GEFs) via phosphorylation; due to large network of overlapping phosphorylation, a multitude of GEFs are utilized to enable specific signaling pathways. These structural arrangements provide interaction sites that can interact with effectors and guanine factors in order to stabilize and signal the hydrolysis of GTP.[8]

Participation in cellular processes
RhoA is primarily involved in these activities: actin organization, myosin contractility, cell cycle maintenance, cellular morphological polarization, cellular development and transcriptional control.

Actin organization
RhoA is prevalent in regulating cell shape, polarity and locomotion via actin polymerization, actomyosin contractility, cell adhesion, and microtubule dynamics. In addition, RhoA is believed to act primarily at the rear (uropod) of migrating cells to promote detachment, similar to the attachment and detachment process found in the focal adhesion mechanism. Signal transduction pathways regulated via RhoA link plasma membrane receptors to focal adhesion formation and the subsequent activation of relevant actin stress fibers. RhoA directly stimulates actin polymerization through activation of diaphanous-related formins, thereby structurally changing the actin monomers to filaments. ROCK kinases induce actomyosin-based contractility and phosphorylate TAU and MAP2 involved in regulating myosins and other actin-binding proteins in order to assist in cell migration and detachment. The concerted action of ROCK and Dia is essential for the regulation of cell polarity and organization of microtubules. RhoA also regulates the integrity of the extracellular matrix and the loss of corresponding cell-cell adhesions (primarily adherens and tight junctions) required for the migration of epithelial. RhoA's role in signal transduction mediation is also attributed to the establishment of tissue polarity in epidermal structures due to its actin polymerization to coordinate vesicular motion;[9] movement within actin filaments forms webs that move in conjunction with vesicular linear motion. As a result, mutations present in the polarity genes indicate that RhoA is critical for tissue polarity and directed intracellular movement.

Cell development
RhoA is required for processes involving cell development, some of which include outgrowth, dorsal closure, bone formation, and myogenesis. Loss of RhoA function is frequently attributed to failed gastrulation and cell migration inability. In extension, RhoA has been shown to function as an intermediary switch within the overall mechanically mediated process of stem cell commitment and differentiation. For example, human mesenchymal stem cells and their differentiation into adipocytes or osteocytes are direct results of RhoA's impact on cell shape, signaling and cytoskeletal integrity. Cell shape acts as the primary mechanical cue that drives RhoA activity and downstream effector ROCK activity to control stem cell commitment and cytoskeletal maintenance.[10] Transforming growth factor (TGF)-mediated pathways that control tumor progression and identity are also frequently noted to be RhoA-dependent mechanisms. TGF-β1, a tumor suppressive growth factor, is known to regulate growth, differentiation and epithelial transformation in tumorigenesis. Instead of blocking growth, TGF-β1 directly activates RhoA in epithelial cells while blocking its downstream target, p160; as a result, activated RhoA-dependent pathways induce stress fiber formation and subsequent mesenchymal properties .[11]

Transcriptional control
Activated RhoA also participates in regulating transcriptional control over other signal transduction pathways via various cellular factors. RhoA proteins help potentiate the transcription independent of ternary complex factors when activated while simultaneously modulating subsequent extracellular signal activity. It has also been shown that RhoA mediates serum-, LPA- and AIF4-induced signaling pathways in addition to regulating the transcription of the c-fos promoter, a key component in the formation of the ternary complex producing the serum and ternary factors.[12] RhoA signaling and modulation of actin polymerization also regulates Sox9 expression via controlling transcriptional Sox9 activity. The expression and transcriptional activity of Sox9 is directly linked with the loss of RhoA activity and illustrates how RhoA participates in the transcriptional control of specific protein expression.[13]

Cell cycle maintenance
RhoA as well as several other members of the Rho family are identified as having roles in the regulation of the cytoskeleton and cell division. RhoA plays a pivotal role in G1 cell cycle progression, primarily through regulation of cyclin D1 and cyclin-dependent kinase inhibitors (p21 and p27) expression. These regulation pathways activate protein kinases, which subsequently modulate transcription factor activity. RhoA specifically suppresses p21 levels in normal and transformed cell lines via a p53-independent transcriptional mechanism while p27 levels are regulated using effector Rho-associated kinases. Cytokinesis is defined by actomyosin-based contraction. RhoA-dependent diaphanous-related formins (DRFs) localize to the cleavage furrow during cytokinesis while stimulating local actin polymerization by coordinating microtubules with actin filaments at the site of the myosin contractile ring. Differences in effector binding distinguish RhoA amongst other related Ras homologs GTPases. Integrins can modulate RhoA activity depending on the extracellular matrix composition and other relevant factors. Similarly, RhoA's stimulation of PKN2 kinase activity regulates cell-cell adhesion through apical junction formation and disassembly.[7][14] Though RhoA is most easily recognized from its unique contributions in actin-myosin contractility and stress fiber formation, new research has also identified it as a key factor in the mediation of membrane ruffling, lamellae formation and membrane blebbing. A majority of this activity occurs in the leading edge of cells during migration in coordination with membrane protrusions of breast carcinoma.[15]

RhoA pathway
Molecules act on various receptors, such as NgR1, LINGO1, p75, TROY and other unknown receptors (e.g. by CSPGs), which stimulates RhoA. RhoA activates ROCK (RhoA kinase) which stimulates LIM kinase, which then inhibits cofilin, which effectively reorganizes the actin cytoskeleton of the cell.[5] In the case of neurons, activation of this pathway results in growth cone collapse, therefore inhibits the growth and repair of neural pathways and axons. Inhibition of this pathway by its various components usually results in some level of improved re-myelination.[16][17][18][19] After global ischemia, hyperbaric oxygen (at least at 3 ATA) appears to partially suppress expression of RhoA, in addition to Nogo protein (Reticulon 4), and a subunit of its receptor Ng-R.[20] The MEMO1-RhoA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. A recent study shows that RhoA-Rho kinase signaling mediates thrombin-induced brain damage.[21]

Interactions
RHOA has been shown to interact with:

ARHGAP1,[22][23][24][25]
ARHGAP5,[26]
ARHGDIA,[27][28][29][30][31]
ARHGEF11,[32]
ARHGEF12,[33]
ARHGEF3,[34]
CIT[35][36]
DGKQ,[37]
DIAPH1,[35]
GEFT,[38]
ITPR1,[35][39]
KCNA2,[40]
KTN1,[41][42][43]
PKN2,[44][45][46]
PLCG1,[47]
Phospholipase D1,[48][49]
Protein kinase N1,[35][45][50]
RAP1GDS1,[51]
RICS,[52][53][53]
ROCK1,[54][55]
TRIO,[56] and
TRPC1.[39]
Clinical significance
Cancer
Given that its overexpression is found in many malignancies, RhoA activity has been linked within several cancer applications due to its significant involvement in cancer signaling cascades. Serum response factors (SRFs) are known to mediate androgen receptors in prostate cancer cells, including roles ranging from distinguishing benign from malignant prostate and identifying aggressive disease. RhoA mediates androgen-responsiveness of these SRF genes; as a result, interference with RhoA has been shown to prevent the androgen regulation of SRF genes. In application, RhoA expression is notably higher in malignant prostate cancer cells compared to benign prostate cells, with elevated RhoA expression being associated with elevated lethality and aggressive proliferation. On the other hand, silencing RhoA lessened androgen-regulated cell viability and handicapped prostate cancer cell migration.[57]

RhoA has also been found to be hyper activated in gastric cancer cells; in consequence, suppression of RhoA activity partially reversed the proliferation phenotype of gastric cancer cells via the down-regulation of the RhoA-mammalian Diaphanous 1 pathway.[58] Doxorubicin has been referred to frequently as a highly-promising anti-cancer drug that is also being utilized in chemotherapy treatments; however, as with nearly all chemotherapeutics, the issue of drug resistance remains. Minimizing or postponing this resistance would the necessary dose to eradicate the tumor, thus diminishing drug toxicity. Subsequent RhoA expression decrease has also been associated with increased sensitivity to doxorubicin and the complete reversion of doxorubicin resistance in certain cells; this shows the resilience of RhoA as a consistent indicator anti-cancer activity. In addition to promoting tumor-suppression activity, RhoA also has inherent impact upon the efficacy of drugs in relation to cancer functionality and could be applied to gene therapy protocols in future research.[59]

Protein expression of RhoA has been identified to be significantly higher in testicular tumor tissue than that in nontumor tissue; expression of protein for RhoA, ROCK-I, ROCK-II, Rac1, and Cdc42 was greater in tumors of higher stages than lower stages, coinciding with greater lymph metastasis and invasion in upper urinary tract cancer. Although both RhoA and RhoC proteins comprise a significant part of the Rho GTPases that are linked to promoting the invasive behavior of breast carcinomas, attributing specific functions to these individual members has been difficult. We have used a stable retroviral RNA interference approach to generate invasive breast carcinoma cells (SUM-159 cells) that lack either RhoA or RhoC expression. Analysis of these cells enabled us to deduce that RhoA impedes and RhoC stimulates invasion. Unexpectedly, this analysis also revealed a compensatory relationship between RhoA and RhoC at the level of both their expression and activation, and a reciprocal relationship between RhoA and Rac1 activation. Chronic Myeloid Leukemia (CML), a stem cell disorder that prevents myeloid cells from functioning correctly, has been linked to actin polymerization. Signaling proteins like RhoA, regulate polymerization of actin. Due to differences proteins exhibited between normal and affected neutrocytes, RhoA has become the key element; further experimentation has also shown that RhoA-inhibiting pathways prevent the overall growth of CML cells. As a result, RhoA has significant potential as a therapeutic target in gene therapy techniques to treating CML.[60] Therefore, RhoA's role in the proliferation of cancer cell phenotypes is a key application that can be applied to targeted cancer therapeutics and the development for pharmaceuticals.

Drug applications
In June 2012, a new drug candidate named "Rhosin" was synthesized by researchers at the Cincinnati Children's Hospital, a drug with the full intention to inhibit cancer proliferation and promote nerve cell regeneration. This inhibitor specifically targets Rho GTPases to prevent cell growth related to cancer. When tested on breast cancer cells, Rhosin inhibited growth and the growth of mammary spheres in a dose dependent manner, functioning as targets for RhoA while simultaneously maintaining the integrity of normal cellular processes and normal breast cells. These promising results indicate Rhosin's general effectiveness in preventing breast cancer proliferation via RhoA targeting.[61]

Possible target for asthma and diabetes drugs
RhoA's physiological functions have been linked to the contraction and migration of cells which are manifested as symptoms in both asthma and diabetes (i.e. airflow limitation and hyper-responsiveness, desensitization, etc.). Due to pathophysiological overlap of RhoA and Rho-kinase in asthma, both RhoA and Rho-kinase have become promising new target molecules for pharmacological research to develop alternate forms of treatment for asthma.[62] RhoA and Rho kinase mechanisms have been linked to diabetes due to the up-regulated expression of targets within type 1 and 2 diabetic animals. Inhibition of this pathway prevented and ameliorated pathologic changes in diabetic complications, indicating that RhoA pathway is a promising target for therapeutic development in diabetes treatment

Zebrafish retina

Zebrafish retina. ELF® 97 Immunohistochemistry Kit, Hoechst 33342 and tetramethylrhodamine wheat germ agglutinin.
A transverse section through adult zebrafish retina that has been probed with anti–glial fibrillary acidic protein antibody (anti-GFAP antibody, Cat. no. A21282) and then developed for visualization with alkaline phosphatase–mediated techniques using our ELF® 97 Immunohistochemistry Kit (Cat. no. E6600). This kit's ELF® 97 phosphatase substrate yields an extremely photostable yellow-green signal at the site of anti-GFAP binding, clearly showing that this antibody binds to Müller cells in the zebrafish retina. The retinal section has been counterstained with Hoechst 33342 (Cat. no. H1399, H3570, H21492), which stains all nuclei blue, and with tetramethylrhodamine wheat germ agglutinin (Cat. no. W849), which stains both the inner and outer plexiform layers as well as the photoreceptor outer segments red.