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Titolo:
Synthesis and post-translational processing of surfactant protein C
Autore:
Solarin, KO; Wang, WJ; Beers, MF;
Indirizzi:
Univ Penn, Sch Med, Dept Med, Div Pulm & Crit Care, Philadelphia, PA 19104USA Univ Penn Philadelphia PA USA 19104 Crit Care, Philadelphia, PA 19104USA Thomas Jefferson Univ, Sch Med, Div Neonatol, Philadelphia, PA 19107 USA Thomas Jefferson Univ Philadelphia PA USA 19107 hiladelphia, PA 19107 USA
Titolo Testata:
PEDIATRIC PATHOLOGY & MOLECULAR MEDICINE
fascicolo: 6, volume: 20, anno: 2001,
pagine: 471 - 500
SICI:
1522-7952(200111/12)20:6<471:SAPPOS>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
BOVINE PULMONARY SURFACTANT; LUNG LAMELLAR BODIES; HUMAN FETAL LUNG; RAT LUNG; SP-B; GLUCOCORTICOID REGULATION; HYDROPHOBIC PROTEINS; INSITU HYBRIDIZATION; TRANSGENIC MICE; MESSENGER-RNAS;
Keywords:
lung epithelial cells; palmitoylation; propeptide processing; surfactant protein C; targeting;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Citazioni:
99
Recensione:
Indirizzi per estratti:
Indirizzo: Beers, MF Univ Penn, Sch Med, Dept Med, Div Pulm & Crit Care, 807 BRB 2-3 Bldg,421 Curie Blvd, Philadelphia, PA 19104 USA Univ Penn 807 BRB 2-3 Bldg,421 Curie Blvd Philadelphia PA USA 19104
Citazione:
K.O. Solarin et al., "Synthesis and post-translational processing of surfactant protein C", PEDIAT PATH, 20(6), 2001, pp. 471-500

Abstract

Traditional thinking about surfactant Proteins has centered around their effects on the biophysical properties of surfactant phospholipids. Accumulated data now suggests that the jour major surfactant proteins (SPs) are a biochemically and functionally diverse group of mammalian peptides that have function beyond modification of alveolar surface tension. Alveolar SP-C (SP-C-3.7, M-r 21,000) is 35 amino acid peptide isolated fi-om lung surfactantthat is synthesized and processed from a 191-197 amino acid precursor (proSP-C-21). Although its solubility in organic solvents and avidity for lipidmembranes impart properties important for its biophysical activity, SP-C represents a structurally and functionally challenging protein for the alveolar type II cell that must synthesize and traffic the peptide through the regulated secretory pathway. Despite technical and analytical difficulties imposed by its unique structure, our current understanding of SP-C biosynthesis has evolved over the past 10 years. Recent data now require its to consider proSP-C-21 as a hybrid molecule incorporating structural and functional features both of bitopic integral membrane proteins as well as more classically recognized propeptide hormones. Our article highlights major developments related to characterization of molecular and cellular mechanisms underlying expression, post-translational processing, and targeting of proSP-C-21 that result in production of secreted SP-C-3.7.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/06/20 alle ore 08:40:07