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Titolo:
PROTEIN-KINASE-A AND PROTEIN-KINASE-C RAPIDLY MODULATE EXPRESSION OF HUMAN LUNG FIBROBLAST B-2 BRADYKININ RECEPTOR AFFINITY FORMS
Autore:
DALEMAR LR; JONG YJI; WILHELM B; BAENZIGER NL;
Indirizzi:
WASHINGTON UNIV,SCH MED,DEPT ANAT & NEUROBIOL,660 S EUCLID AVE,BOX 8108 ST LOUIS MO 63110 WASHINGTON UNIV,SCH MED,DEPT ANAT & NEUROBIOL ST LOUIS MO 63110
Titolo Testata:
European journal of cell biology
fascicolo: 3, volume: 69, anno: 1996,
pagine: 236 - 244
SICI:
0171-9335(1996)69:3<236:PAPRME>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
SWISS 3T3 FIBROBLASTS; CANINE KIDNEY-CELLS; PHORBOL ESTER; ADENYLATE-CYCLASE; BETA-2-ADRENERGIC RECEPTOR; TYROSINE PHOSPHORYLATION; PROSTAGLANDIN SYNTHESIS; SIGNAL-TRANSDUCTION; RAS ONCOGENE; ACTIVATION;
Keywords:
BRADYKININ RECEPTOR; INDUCTION; MONOCLONAL ANTIBODIES; PROTEIN KINASE C; PROTEIN KINASE A;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
54
Recensione:
Indirizzi per estratti:
Citazione:
L.R. Dalemar et al., "PROTEIN-KINASE-A AND PROTEIN-KINASE-C RAPIDLY MODULATE EXPRESSION OF HUMAN LUNG FIBROBLAST B-2 BRADYKININ RECEPTOR AFFINITY FORMS", European journal of cell biology, 69(3), 1996, pp. 236-244

Abstract

WI-38 and IMR90 human lung fibroblasts express Bt receptors for the peptide mediator bradykinin. These G-protein-coupled receptors which control cell growth, protein synthesis, and prostaglandin E(2) (PGE(2)) production occur in three affinity forms, high (H, K-D 440 pM), intermediate (I, K-D 5.6 nM), and low (L, K-D nM). Utilizing specific monoclonal antireceptor antibodies which are able to distinguish among theseB-2 bradykinin receptor forms, we demonstrate regulated differential enhancement of their expression in fibroblasts. Activation of cellularsecond messenger regulatory pathways based on protein kinase C or protein kinase A drives B-2 receptor affinity form expression in oppositedirections, both of which are relevant to the levels of human bradykinin generation in vivo in the tissues of origin for these fibroblasts. On a spontaneous basis WI-38 human lung fibroblasts most frequently express the L form alone or the I+L forms concurrently. Activation of protein kinase C augments expression of both I and L affinity receptorswithin 30 min, increasing receptor number and enhancing PGE(2) production. In contrast, activation of protein kinase A by 8-bromo-cAMP or forskolin enhances receptor expression and PGE(2) production instead atthe I to H types of affinity forms within 30 min. The effects of bothkinase systems are blocked by serine/threonine (Ser/Thr) protein kinase inhibitors, indicating a role for phosphorylation at Ser or Thr residues in determining the cellular expression of bradykinin B-2 receptor affinity forms. An increase in immunoprecipitable I form bradykinin receptors is detectable within 20 to 30 min after activation of eitherprotein kinase C or protein kinase A. This time frame emphasizes the ability of human fibroblasts for rapid mobilization of B-2 receptor affinity forms. Regulated expression of this repertoire of bradykinin B-2 receptors at the level of receptor number and concurrent activity allows fibroblasts a sensitive means to adjust their responses to their cellular environment utilizing Ser/Thr phosphorylation events.

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Documento generato il 29/09/20 alle ore 16:44:17