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酸性蛋白酶作用于哺乳动物白蛋白所形成的组胺释放肽的结构

Structures of histamine-releasing peptides formed by the action of acid proteases on mammalian albumin(s).

作者信息

Carraway R E, Cochrane D E, Boucher W, Mitra S P

机构信息

Department of Physiology, University of Massachusetts Medical School, Worcester 01655.

出版信息

J Immunol. 1989 Sep 1;143(5):1680-4.

PMID:2474609
Abstract

The acid proteases, pepsin, rennin and cathepsin D, were shown to generate mast cell histamine releasing peptides (HRP) when incubated with the albumin fraction of mammalian plasmas. Significant histamine release was observed using less than 1 microliter equivalent of pepsin-treated plasma. Histamine release was rapid, dependent on calcium and energy, and accompanied by degranulation. The major HRP present in pepsin-treated human and canine plasma was identified as H-Ile-Ala-Arg-Arg-His-Pro-Tyr-Phe-OH whereas that from rat plasma had valine substituted for isoleucine. Cathepsin D-treated BSA gave rise to the human octapeptide (above) as well as to an extended decapeptide with H-Tyr-Glu- at the N-terminus. These peptides were apparently derived from one region of serum albumin, residues 139 to 149 of the human, canine, or bovine sequence. We hypothesize that cathepsin D, released from leukocyte lysosomes, might generate HRP during the delayed phase of an inflammatory response.

摘要

酸性蛋白酶、胃蛋白酶、凝乳酶和组织蛋白酶D,在与哺乳动物血浆的白蛋白部分一起孵育时,会产生肥大细胞组胺释放肽(HRP)。使用不到1微升等效的胃蛋白酶处理血浆即可观察到显著的组胺释放。组胺释放迅速,依赖于钙和能量,并伴有脱颗粒现象。胃蛋白酶处理的人血浆和犬血浆中存在的主要HRP被鉴定为H-Ile-Ala-Arg-Arg-His-Pro-Tyr-Phe-OH,而大鼠血浆中的HRP则是缬氨酸取代了异亮氨酸。组织蛋白酶D处理的牛血清白蛋白产生了上述人源八肽以及N端带有H-Tyr-Glu-的延伸十肽。这些肽显然来源于血清白蛋白的一个区域,即人、犬或牛序列的139至149位残基。我们推测,从白细胞溶酶体释放的组织蛋白酶D可能在炎症反应的延迟期产生HRP。

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