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The 180-kD component of the neural cell adhesion molecule N-CAM is involved in cell-cell contacts and cytoskeleton-membrane interactions (1987)

Pollerberg, G. Elisabeth ; Burridge, Keith ; Krebs, Keith E. ; [et al.]

Springer

Cell & tissue research 250 (1987), S. 227-236

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ISSN: 1432-0878

Keywords: Brain spectrin ; Cell interactions ; Cytoskeleton ; Neural cell adhesion molecule N-CAM ; Neural cell culture

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine

Notes: Summary N-CAM180, the molecular form of the three neural cell adhesion molecules (N-CAM) with the largest cytoplasmic domain, is accumulated at sites of cell-cell contact (cell bodies, neurites, growth cones) in cultures of neuroblastoma and cerebellum. At these sites the cytoskeletonmembrane linker protein brain spectrin and actin are also accumulated. Brain spectrin copurifies with N-CAM180 by immunoaffinity chromatography and binds specifically to N-CAM180 but not to N-CAM140 or N-CAM120 in a solid-phase binding test. These observations indicate an association of N-CAM180 with the cytoskeleton in vivo. This association may underlie the reduced lateral mobility of N-CAM180 in the surface membrane compared to N-CAM140 (Pollerberg et al. 1986). Together with the fact that N-CAM180 is only expressed after termination of neuron migration in vivo (Persohn and Schachner, unpublished) these results suggest a role for N-CAM180 in stabilization of cell contacts.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00214676

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Demonstration of a relationship between talin and P235, a major substrate of the calcium-dependent protease in platelets (1986)

Beckerle, Mary C. ; O'Halloran, Theresa ; Burridge, Keith

New York, N.Y. : Wiley-Blackwell

Journal of Cellular Biochemistry 30 (1986), S. 259-270

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ISSN: 0730-2312

Keywords: actin-membrane ; interactions ; Ca++-activated proteolysis ; talin ; platelets ; calcium dependent protease ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: Talin is a 225,000-Dalton protein we have purified from smooth muscle. In chick embryo fibroblasts talin is found in adhesion plaques (focal contacts), areas where the cell is closely opposed to the substratum. In comparison with other cytoskeletal proteins, we found talin to be unusually susceptible to proteolysis and have identified a 190,000-Dalton proteolytic fragment of talin in the immunoblots of many tissues. These observations raised the possibility that the cleavage of talin to this fragment has physiological relevance. One system that we have investigated in which significant proteolysis occurs is platelets. During platelet activation several high-molecular-weight proteins are cleaved to lower-molecular-weight forms. Here we demonstrate that talin is closely related to one of these platelet high-molecular-weight proteins, P235. The purification of talin is comparable to that developed for P235, and the two proteins have similar biophysical properties. In addition, antibodies raised against chicken gizzard talin recognize P235 in purified form as well as in crude platelet extracts. The platelet protein also resembles smooth-muscle talin in its susceptibility to endogenous proteolysis: P235 is rapidly cleaved to a 190-200kD polypeptide by a calcium-activated protease found in platelet extracts. Moreover, partial proteolysis of P235 and talin with chymotrypsin, elastase, or trypsin also generates remarkably similar one-dimensional peptide maps. Because of their similar biophysical properties, immunological crossreactivity, and similar one-dimensional partial peptide maps, we conclude that P235 is the platelet form of talin.

Additional Material: 5 Ill.