The Chromaffin Vesicle: Advances in Understanding the Composition of a Versatile, Multifunctional Secretory Organelle

被引:48
作者
Crivellato, Enrico [1 ]
Nico, Beatrice [2 ]
Ribatti, Domenico [2 ]
机构
[1] Univ Udine, Sch Med, Dept Med & Morphol Res, Anat Sect, I-33100 Udine, Italy
[2] Univ Bari, Sch Med, Dept Human Anat & Histol, Bari, Italy
来源
ANATOMICAL RECORD-ADVANCES IN INTEGRATIVE ANATOMY AND EVOLUTIONARY BIOLOGY | 2008年 / 291卷 / 12期
关键词
chromaffin vesicle; molecular content; stress response;
D O I
10.1002/ar.20763
中图分类号
R602 [外科病理学、解剖学]; R32 [人体形态学];
学科分类号
100101 ;
摘要
Chromaffin vesicles (CV) are highly sophisticated secretory organelles synthesized in adrenal medullary chromaffin cells. They contain a complex mixture of structural proteins, catecholamine neurotransmitters, peptide hormones, and the relative processing enzymes, as well as protease inhibitors. In addition, CV store ATP, ascorbic acid, and calcium. During the last decades, extensive studies have contributed to increase our understanding of the molecular composition of CV. Yet, the recent development of biochemical and imaging procedures has greatly increased the list of CV-soluble constituents and opened new horizons as to the complexity of CV involvement in acute stress responses. Thus, a coherent picture of CV molecular composition is still to be drawn. This review article will provide a detailed account of the content of CV soluble molecules as it emerges from the most recent analytical studies. Moreover, this review article will attempt at focussing on the physiological and pathophysiological implications of the products released by CV. Anat Rec, 291:1587-1602, 2008. (C) 2008 Wiley-Liss, Inc.
引用
收藏
页码:1587 / 1602
页数:16
相关论文
共 131 条
[1]  
[Anonymous], 1939, J PHYSL
[2]   Identification of a novel secretogranin II-derived peptide (SgII187-252) in adult and fetal human adrenal glands using antibodies raised against the human recombinant peptide [J].
Anouar, Y ;
Desmoucelles, C ;
Yon, L ;
Leprince, J ;
Breault, L ;
Gallo-Payet, N ;
Vaudry, H .
JOURNAL OF CLINICAL ENDOCRINOLOGY & METABOLISM, 1998, 83 (08) :2944-2951
[3]   Exocytosis in chromaffin cell of the adrenal medulla [J].
Aunis, D .
INTERNATIONAL REVIEW OF CYTOLOGY - A SURVEY OF CELL BIOLOGY, VOL 181, 1998, 181 :213-320
[4]  
AZARYAN AV, 1995, J NEUROCHEM, V65, P1771
[5]   PURIFICATION AND CHARACTERISTICS OF THE CANDIDATE PROHORMONE PROCESSING PROTEASES PC2 AND PC1/3 FROM BOVINE ADRENAL-MEDULLA CHROMAFFIN GRANULES [J].
AZARYAN, AV ;
KRIEGER, TJ ;
HOOK, VYH .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (14) :8201-8208
[6]  
BABINSKI K, 1995, J NEUROCHEM, V64, P1080
[7]   Expression of regulated secretory proteins is sufficient to generate granule-like structures in constitutively secreting cells [J].
Beuret, N ;
Stettler, H ;
Renold, A ;
Rutishauser, J ;
Spiess, M .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (19) :20242-20249
[8]  
BLASCHKO H, 1953, N-S ARCH EX PATH PH, V219, P17
[9]   HETEROGENEITY IN THE ADRENOMEDULLARY STORAGE OF CATECHOLAMINES, ATP, CALCIUM AND RELEASABLE DOPAMINE BETA-HYDROXYLASE ACTIVITY [J].
BOLSTAD, G ;
HELLE, KB ;
SERCKHANSSEN, G .
JOURNAL OF THE AUTONOMIC NERVOUS SYSTEM, 1980, 2 (04) :337-354
[10]   Role of prohormone convertases in pro-neuropeptide Y processing:: Coexpression and in vitro kinetic investigations [J].
Brakch, N ;
Rist, B ;
Beck-Sickinger, AG ;
Goenaga, J ;
Wittek, R ;
Bürger, E ;
Brunner, HR ;
Grouzmann, E .
BIOCHEMISTRY, 1997, 36 (51) :16309-16320