Characterization of sponge aggregation factor. Unique proteoglycan complex

Henkart, Pierre A.; Humphreys, Susie; Humphreys, Tom

doi:10.1021/bi00740a016

Cited by 209 publications

(94 citation statements)

References 26 publications

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“…As previously reported, the cellaggregating effect of the retina cell-aggregating factor is rapidly destroyed by trypsin (10,11), but is insensitive to It, therefore, appears that the activity of the retina cellaggregating glycoprotein depends on the integrity of the protein moiety, but not on retention of the terminal sialic-acid residues, on the galactose residues, or on those sugar residues that are sensitive to oxidation with periodate under these conditions. It is noteworthy that the cell aggregation factors of mouse teratoma (26) and of marine sponges (27,28) have a much higher carbohydrate content; the latter show considerable resistance to trypsin but are inactivated by Pronase (29,30) and periodate (31), and, therefore, were suggested to require the polysaccharide moiety for their characteristic effect (31).…”

Section: Resultsmentioning

confidence: 99%

Purification and characterization of the retina-specific cell-aggregating factor.

Hausman¹,

Moscona²

1975

Proc. Natl. Acad. Sci. U.S.A.

125

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The tissue-specific, cell-aggregating component of embryonic neural retina cells was purified from the retina* cell-aggregating factor and characterized as a glycoprotein. Its molecular weight in solution is in the range of 50,000, and it contains 10-15% carbohydrate. The amino-acid and carbohydrate compositions hlave been determined. The glycoprotein is produced by embryonic neural retina cells in primary monolayered cultures and is released into the medium. Its tissue-specific, cell-aggregating effect requires integrity of the polypeptide portion, but not of the carbohydrate portion. We suggest that the isolated molecule is a specific determinant of the embryonic retina cell-surface and that it is involved in mediating self-recognition and selective adhesiveness of these cells.

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Section: Resultsmentioning

confidence: 99%

Purification and characterization of the retina-specific cell-aggregating factor.

Hausman¹,

Moscona²

1975

Proc. Natl. Acad. Sci. U.S.A.

125

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“…Many workers have associated cell surface glycoproteins with adhesion-related activities in systems such as sponges (9), slime molds (19,27), and avian and mammalian cells (7,28,36). Our fording that the function of an adhesive organelle, the desmosome, may be mediated by certain glycoproteins is also supported by ultrastructural localization of carbohydrate in the intercellular region of desmosomes, using various histochemical stains such as ruthenium red (11), phosphotungstic acid (8), and periodic acid-silver methenamine (8,22).…”

Section: Discussionmentioning

confidence: 99%

Isolation of the intercellular glycoproteins of desmosomes.

Gorbsky

Steinberg

1981

The Journal of Cell Biology

204

111

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To characterize the desmosome components that mediate intercellular adhesion and cytoskeletal-plasma membrane attachment, we prepared whole desmosomes and isolated desmosomal intercellular regions (desmosomal "cores") from the living cell layers of bovine muzzle epidermis. The tissue was disrupted in a nonionic detergent at low pH, sonicated, and the insoluble residue fractionated by differential centrifugation and metrizamide gradient centrifugation. Transmission electron microscopic analyses reveal that a fraction obtained after differential centrifugation is greatly enriched in whole desmosomes that possess intracellular plaques. Metrizamide gradient centrifugation removes most of the plaque material, leaving the intercellular components and the adjoining plasma membranes. Sodium dodecyl sulfate polyacrylamide gel electrophoresis coupled with methods that reveal carbohydrate-containing moieties on gels demonstrate that certain proteins present in whole desmosomes are glycosylated. These glycoproteins are specifically and greatly enriched in the desmosome cores of which they are the principal protein constituents, and thus may function as the intercellular adhesive of the desmosome.

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“…In systems involving adhesion of identical cells, additional theoretical considerations and biophysical parameters have been proposed (17-21). Current research in cellular recognition is centered on the identification and characterization of cell-surface aggregation factors isolated from diverse systems (22)(23)(24)(25)(26)(27)(28)(29)(30)(31)(32)(33). In general, the information for the specificity of aggregation factors is considered to reside in the primary sequence of the protein moiety.…”

Section: Introductionmentioning

confidence: 99%

Molecular Complementarity of Yeast Glycoprotein Mating Factors

Crandall

Lawrence

Saunders

1974

Proc. Natl. Acad. Sci. U.S.A.

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Cell fusion between opposite mating types 5 and 21 of the yeast Hansenula wingei is initiated by a strong sexual agglutination reaction. The mating factors responsible for the specificity of cellular recognition are complementary glycoproteins which form a physical complex in vitro. The complex is assayed by recovery of agglutination activity of the multivalent 5-factor after the univalent 21-factor has been inactivated by treatment of the complex with alkali. The 5-factor 21-factor complex, purified on Sepharose 6B, is large (several million daltons) and heterogeneous. The three peaks of 5-factor activity contain a number of combining sites proportional to molecular size.In this paper, evidence is presented for complex formation in vitro between yeast glycoprotein mating factors. These cellwall factors determine the specificity of cellular recognition as the first step in mating. Thus, these factors may be considered "complementary" in the sense proposed by Emil Fisher (1) in his-analogy:... "dass Enzym und Glucosid wie Schloss und Schlussel" .... Shortly later, in 1913, Lillie (2) described an activity extracted from sea-urchin eggs that specifically agglutinated sperm cells and was therefore complementary to a sperm-surface component. These early ideas concerning preformed combining sites on macromolecules formed the basis of models proposed by Tyler (3) and Weiss (4) in which the specificity of cellular adhesion in tissue development was explained by the presence of complementary molecules on opposing cell surfaces which combined in a manner analogous to antigen-antibody complex formation. Subsequent studies of cell contact have been reviewed extensively (see refs. 5-16 and other papers in these volumes). In systems involving adhesion of identical cells, additional theoretical considerations and biophysical parameters have been proposed (17-21). Current research in cellular recognition is centered on the identification and characterization of cell-surface aggregation factors isolated from diverse systems (22)(23)(24)(25)(26)(27)(28)(29)(30)(31)(32)(33). In general, the information for the specificity of aggregation factors is considered to reside in the primary sequence of the protein moiety. However, the role played by the carbohydrate moieties may be nontrivial since most of the aggregation factors studied thus far either interact with carbohydrates or glycoproteins on the cell surface or are glycoproteins themselves. The latter is true for the mating factors isolated from sexually agglutinative mating types of the yeast Hansenula wingei (34). This mating system has been reviewed (34), and criteria for determining specificity in other cell-aggregating systems were proposed (35). The hypothesis that the haploid mating factors are mutually repressed in the nonagglutinative diploid (36) has been supported by recent work in which conditions for the differential induction of each glycoprotein mating factor in the diploid were discovered (37).The mating factor from strain 5, called 5-factor (5f) (38) or ...

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Characterization of sponge aggregation factor. Unique proteoglycan complex

Cited by 209 publications

References 26 publications

Purification and characterization of the retina-specific cell-aggregating factor.

Purification and characterization of the retina-specific cell-aggregating factor.

Isolation of the intercellular glycoproteins of desmosomes.

Molecular Complementarity of Yeast Glycoprotein Mating Factors

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