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Titolo:
PROTEASE-RESISTANT L-SELECTIN MUTANTS - DOWN-MODULATION BY CROSS-LINKING BUT NOT CELLULAR ACTIVATION
Autore:
STODDART JH; JASUJA RR; SIKORSKI MA; VONANDRIAN UH; MIER JW;
Indirizzi:
TUFTS UNIV NEW ENGLAND MED CTR,DEPT MED,TUPPER RES INST,750 WASHINGTON ST BOSTON MA 02111 TUFTS UNIV NEW ENGLAND MED CTR,DEPT MED,TUPPER RES INST BOSTON MA 02111 TUFTS UNIV NEW ENGLAND MED CTR,DIV HEMATOL ONCOL BOSTON MA 02111 HARVARD UNIV,SCH MED,CTR BLOOD RES BOSTON MA 02115
Titolo Testata:
The Journal of immunology
fascicolo: 12, volume: 157, anno: 1996,
pagine: 5653 - 5659
SICI:
0022-1767(1996)157:12<5653:PLM-DB>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
LEUKOCYTE ADHESION MOLECULE-1; MEMBRANE-PROXIMAL CLEAVAGE; HIGH ENDOTHELIAL VENULES; HUMAN NEUTROPHILS; CHROMOSOMAL LOCALIZATION; CHEMOTACTIC FACTORS; SURFACE MOLECULE; HOMING RECEPTORS; PROTEINS; INVITRO;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
J.H. Stoddart et al., "PROTEASE-RESISTANT L-SELECTIN MUTANTS - DOWN-MODULATION BY CROSS-LINKING BUT NOT CELLULAR ACTIVATION", The Journal of immunology, 157(12), 1996, pp. 5653-5659

Abstract

The adhesion molecule L-selectin (CD62L) is rapidly shed from the plasma membrane during leukocyte activation as a result of proteolytic cleavage between Lys(321) and Ser(322) within the extracellular domain, L-selectin is also down-modulated from the surface in response to cross-linking, possibly through a similar mechanism. To further characterize the mechanism of downmodulation, several L-selectin mutants were generated and transfected into COS cells, Wild-type L-selectin as well as mutants with one or two amino acid substitutions at the cleavage site were nearly quantitatively shed into the culture supernatant. However, mutants in which a nine-amino acid stretch that included the protease-sensitive site was either deleted or replaced with a polyglycine spacer or a comparable region of E-selectin were retained on the cell surface and not detected in the supernatant, These results are consistent with other reports describing protease resistant L-selectin mutants. We also demonstrate that when expressed in L1-2 pre-B cells, the L-selectin nine-amino acid deletion mutant (321del.9), but not wild-type L-selectin, is resistant to down-regulation induced by PMA. However, both wild-type and mutant 321del.9 are completely lost from the cell surface in response to cross-linking with an L-selectin Ab. PMA-induced- but not L-selectin cross-linking-induced down-modulation was inhibitedby staurosporine. These data are consistent with the idea that the L-selectin protease(s) can tolerate minor structural alterations at the cleavage site, and that L-selectin down-modulation can be induced by more than one mechanism, at least one of which (cross-linking) is protein kinase C independent.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/21 alle ore 09:50:50