Systematic analysis of structures, localization, formation and biological a
ctivities of endogenous peptides derived from functional proteins, such as
hemoglobin, myelin basic protein, immunoglobulins, etc., allowed establishi
ng the basic features of that group of compounds. The sets of these peptide
s 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 t
he action of carboxy- and amino-peptidases. As a result, the families of st
ructurally related families of peptides are generated. The fragments of fun
ctional proteins exhibit a wide range of the biological effects, characteri
stic both for hormones and parahormones, from hormone-releasing to growth-r
egulatory activity. At the same time, the molecular mechanisms of action of
the majority of such peptides are unknown. On the basis of the data obtain
ed the components of tissue-specific peptide pools are considered to form a
novel regulatory system, complementary to other peptidergic systems such a
s hormonal, nervous, immune, etc. The biological role of the fragments of f
unctional proteins in vivo and the patterns of interaction with other regul
atory systems are suggested.