Fragments of functional proteins: role in endocrine regulation

Systematic analysis of structures, localization, formation and biological activities of endogenous peptides derived from functional proteins, such as hemoglobin, myelin basic protein, immunoglobulins, etc., allowed establishing the basic features of that group of compounds. The sets of these peptide...

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Bibliographic Details
Published in:Neurochemical research 1999-09, Vol.24 (9), p.1117-1124
Main Authors: Karelin, A A, Blishchenko EYu, Ivanov, V T
Format: Article
Language:English
Subjects:
aminopeptidase
Animals
carboxypeptidase
Endocrine Glands - physiology
Humans
neuropeptides
Peptide Fragments - physiology
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Summary:Systematic analysis of structures, localization, formation and biological activities of endogenous peptides derived from functional proteins, such as hemoglobin, myelin basic protein, immunoglobulins, etc., allowed establishing the basic features of that group of compounds. The sets of these peptides in mammalian tissues, or "tissue-specific peptide pools" are: (i) tissue specific; (ii) stable at normal conditions; (iii) conservative in the same tissues of different mammalian species; (iv) dependent on the general state of homeostasis of tissue or the whole organism. Formation of such peptides has features of both conformation and site specificity and also involves the action of carboxy- and amino-peptidases. As a result, the families of structurally related families of peptides are generated. The fragments of functional proteins exhibit a wide range of the biological effects, characteristic both for hormones and parahormones, from hormone-releasing to growth-regulatory activity. At the same time, the molecular mechanisms of action of the majority of such peptides are unknown. On the basis of the data obtained the components of tissue-specific peptide pools are considered to form a novel regulatory system, complementary to other peptidergic systems such as hormonal, nervous, immune, etc. The biological role of the fragments of functional proteins in vivo and the patterns of interaction with other regulatory systems are suggested.
ISSN:0364-3190
1573-6903
DOI:10.1023/A:1020756202644