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Titolo:
Structural organization and classification of the human mucin genes
Autore:
Moniaux, N; Escande, F; Porchet, N; Aubert, JP; Batra, SK;
Indirizzi:
Univ Nebraska, Med Ctr, Eppley Inst Res Canc & Allied Dis, Dept Biochem & Mol Biol,Nebraska Med Ctr 984525, Omaha, NE 68198 USA Univ Nebraska Omaha NE USA 68198 aska Med Ctr 984525, Omaha, NE 68198 USA INSERM, U377, F-59045 Lille, France INSERM Lille France F-59045INSERM, U377, F-59045 Lille, France Ctr Hosp Reg & Univ Lille, Hop Huriez, Lab Biochim & Biol Mol, F-59037 Lille, France Ctr Hosp Reg & Univ Lille Lille France F-59037 ol, F-59037 Lille, France
Titolo Testata:
FRONTIERS IN BIOSCIENCE
, volume: 6, anno: 2001,
pagine: D1192 - D1206
SICI:
1093-9946(200110)6:<D1192:SOACOT>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN SALIVARY MUCIN; PORCINE SUBMAXILLARY MUCIN; HUMAN INTESTINAL MUCIN; CARCINOMA-ASSOCIATED ANTIGEN; HUMAN GASTRIC MUCIN; IMMUNODEFICIENCY-VIRUS TYPE-1; POLYMORPHIC EPITHELIAL MUCIN; MAMMARY ADENOCARCINOMA CELLS; CARBOXYL-TERMINAL SEQUENCE; GROWTH-FACTOR SUPERFAMILY;
Keywords:
mucin; relation structure-function; EGF-like domaine; TGF beta-like domain; secreted; membrane-bound; cystin knot domain; review;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
153
Recensione:
Indirizzi per estratti:
Indirizzo: Batra, SK Univ Nebraska, Med Ctr, Eppley Inst Res Canc & Allied Dis, Dept Biochem & Mol Biol,Nebraska Med Ctr 984525, Omaha, NE 68198 USA Univ Nebraska Omaha NE USA 68198 tr 984525, Omaha, NE 68198 USA
Citazione:
N. Moniaux et al., "Structural organization and classification of the human mucin genes", FRONT BIOSC, 6, 2001, pp. D1192-D1206

Abstract

The cells of living organisms in contact with the external environment areconstantly attacked by different kinds of substances such as micro-organisms, toxins, and pollutants. With evolution, defense mechanisms, such as thesecretion of mucus has been developed. Mucins are the main components of mucus. They are synthesized and secreted by specialized cells of the epithelium and in some case, by non mucin-secreting cells. Little was known about the structure of mucins until a decade ago. This is principally due to heavy glycosylation of mucins, which complicated their analysis. With the application of molecular biological methods, structures of the mucin core peptides (apomucins) are beginning to be elucidated. A total of eleven human mucin (MUC) genes have been identified and numbered in chronological order of their description: MUC1-4, MUC5AC, MUC5B, MUC6-8, and MUC11-12. Of these, the complete cDNA sequence are published only for six mucins MUC1, MUC2, MUC4, MUC5B, MUC5AC, and MUC7. Human mucin genes, in general, show three commonfeatures: I) a nucleotide tandem repeat domain; II) a predicted peptide domain containing a high percentage of serines and threonines; III) complex RNA expression. The tandem repeats in mucins make up the majority of the backbone. Related to their structure, mucins can be classified in three distinct subfamilies: gel-forming, soluble, and membrane-bound. Each member from one family possesses common characteristics and probably specific functions. For a long time, they were thought to have the unique function of protecting and lubricating the epithelial surfaces. The study of the mucins structure as well as the relationship between structure and function show that mucins also possess other important functions, such as growth, direct implication in the fetal development, the epithelial renewal and differentiation, the epithelial integrity, carcinogenesis, and metastasis. This review presents the actual knowledge on the mucins structure and the best-characterizedfunction related to their structure.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/04/20 alle ore 09:04:30