Significance of two desmosome plaque-associated polypeptides of molecular weights 75 000 and 83 000.

Franke, Werner W.; Mueller, H.; Mittnacht, Sybille; Kapprell, Hans-Peter; Jorcano, J. L.

doi:10.1002/j.1460-2075.1983.tb01725.x

Cited by 60 publications

(39 citation statements)

References 42 publications

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“…DP III and DP IV differ from each other and from DP I/II, as shown by peptide mapping, absence of immunological cross-reactivity (refs. 7 and 12 and this report), and analysis of in vitro translation products of bovine epidermal mRNA (12). Although an antiserum raised by Cowin and Garrod (25) against DP III reacts with both DP III and DP IV, this has presumably resulted from incomplete separation of the two closely spaced antigens and the omission of cross-adsorption of the antiserum against the lower band, a possibility these authors have recognized.…”

Section: Discussionmentioning

confidence: 89%

“…Two of the proteins that have molecular masses of >200 kDa have been shown to be structurally closely related by both immunological criteria and peptide mapping analysis (7). The other 2 non-glycosylated proteins differ greatly both from the former proteins and from each other as shown by immunoblot labeling patterns, tryptic peptide mapping, isoelectric point comparisons, and biochemical characterization of in vitro translation products of bovine epidermal mRNA (7,12). Estimates of the apparent molecular weights of corresponding desmosomal proteins differ somewhat (see table I in ref.…”

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confidence: 99%

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Isolation of the non-glycosylated proteins of desmosomes and immunolocalization of a third plaque protein: desmoplakin III.

Gorbsky¹,

Cohen²,

Shida³

et al. 1985

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

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The cytoplasmic plaque of the spot desmosome or macula adhaerens mediates the attachment of bundles of intermediate filaments to the plasma membrane. We have isolated from a bovine epidermal desmosome preparation a fraction that is highly enriched in the non-glycosylated desmosomal proteins. Plastic-embedded and thin-sectioned high-speed pellets of this fraction reveal closely packed filaments that resemble plaque regions of the low pH whole desmosome preparation from which they are derived. NaDodSO4/polyacrylamide gel electrophoresis reveals four major, non-glycosylated proteins of 240, 210, 81, and 77 kDa. In agreement with a previous study, we find the 240-and 210-kDa proteins (desmoplakins I and II) to be closely related, whereas the 81-and 77-kDa proteins are unique. This is shown both immunologically and by one-dimensional proteolytic peptide mapping. Monospecific, polyclonal rabbit antibodies were prepared against the 81-kDa protein and used, in conjunction with protein A-complexed colloidal gold particles (PAG), to immunolocalize this antigen on ultrathin sections of bovine muzzle epidermis. On antibody-labeled sections, PAG particles were associated principally with the desmosomal cytoplasmic plaque. Sections exposed to preimmune serum showed little or no labeling. We conclude that the 81-kDa protein, like the 240/210-kDa protein family, is one of the major components of the desmosomal plaque. We designate it as "desmoplakin III." The location of the 77-kDa protein remains to be definitively established.

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Section: Discussionmentioning

confidence: 89%

mentioning

confidence: 99%

Isolation of the non-glycosylated proteins of desmosomes and immunolocalization of a third plaque protein: desmoplakin III.

Gorbsky¹,

Cohen²,

Shida³

et al. 1985

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

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“…Although morphological changes in the keratin filament network have been associated with terminal differentiation, they have not been positively linked with the appearance of these large keratins. Such changes include the interaction between keratin filaments and desmosomal plaques (33)(34)(35)(36)(37)(38), and the formation of bundles (macrofibrils) of keratin filaments (39,40). Nonethless, the finding that large keratins are expressed in all vertebrate epidermis and primarily in epidermis rather than internal epithelia, suggests that…”

Section: Discussionmentioning

confidence: 99%

Expression of unusually large keratins during terminal differentiation: balance of type I and type II keratins is not disrupted.

Kim¹,

Marchuk²,

Fuchs³

1984

The Journal of Cell Biology

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When a basal epidermal cell undergoes a commitment to terminally differentiate, it ceases to divide and begins to migrate outward towards the surface of the skin. Dramatic changes in its cytoskeletal architecture take place, accompanied by numerous changes in the expression of keratins, a family of related polypeptides that form 8-nm filaments in these cells. We show here that a shift to the synthesis of unusually large keratins occurs that does not seem to disrupt the ratio of two distinct subfamilies of keratins. Preliminary studies indicate that this differentiation-specific shift may be at the level of transcriptional rather than post-trancriptional regulation. The striking similarities between these large keratins and the type I and type II keratins of basal epidermal cells suggests the important role that both classes of large keratin sequences must play in the assembly of the intermediate filaments within the differentiating keratinocyte.Several laboratories have reported differences between the keratins of stratum corneum and those of the living layers of epidermis (1--4). During the course of terminal differentiation, changes occur in the expression of the keratin polypeptides that comprise the 8-nm tonofilaments (5-10). For the human, keratins of size 46, 48.5, 50, 52, 56, and 58 kd are synthesized by the basal epidermal cells (Fig. 1, lane 1), whereas additional keratins of size 67, 65.5, and 56.5 kd are produced by the terminally differentiating epidermis (lane 3). As the cells pass through the granular layer to the stratum corneum, a slight reduction in the size of the keratins takes place. As judged by in vitro translation of mRNAs isolated from basal (lane 2) and differentiating (lane 4) keratinocytes, the changes in keratin pattern that occur early in the course of terminal differentiation are clearly at the level of mRNA biosynthesis (5).Recently, it was demonstrated that the keratins produced by basal epidermal cells can be divided into two distinct groups based on the ability of their mRNAs to cross-hybridize with two different cloned keratin cDNAs (11). Other epithelia express different subsets of keratins, but most if not all of these seem to be similar to one or the other of the two epidermal keratin subfamilies (12). The small (40-52 kd) and relatively acidic keratins have been named the type I class, and the large (53-58 kd) and more basic keratins have been named the type II class (13,14). At least one member of each of the two keratin types seem to be expressed in all cells at all times, suggesting their combined importance in filament assembly (14). Sequence analyses (13,(15)(16)(17)(18) have shown that while the two types of keratins share only low (<30%) homology, their predicted secondary structures are strikingly similar and are compatible with their playing an essential role in forming the coiled-coil backbone of the protofilament of the 8-nm keratin filament (13,18).The keratins typical of terminally differentiating keratinocytes seem to be unusually large and are not fo...

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“…Bands 5 ( ∼ 83 kDa) and 6 ( ∼ 75 kDa) also corresponded to proteins that localized within the intracellular plaque, but differed biochemically from each other and other desmosomal constituents (Franke et al, 1983;Cowin & Garrod, 1983). An in vitro translation experiment, the fi rst reported effort to characterize mRNA encoding a desmosomal component, provided further evidence that Bands 5 and 6 were likely products of distinct genes rather than proteolytic or transcriptional variants of the same protein (Franke et al, 1983). Subsequent studies began referring to Bands 5 and 6 as plakoglobin and plakophilin, respectively (Cowin et al, 1986;Schmidt et al, 1994).…”

Section: R M Harmon and K J Greenmentioning

confidence: 93%

Structural and Functional Diversity of Desmosomes

Harmon

Green

2013

Cell Communication & Adhesion

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Significance of two desmosome plaque-associated polypeptides of molecular weights 75 000 and 83 000.

Cited by 60 publications

References 42 publications

Isolation of the non-glycosylated proteins of desmosomes and immunolocalization of a third plaque protein: desmoplakin III.

Isolation of the non-glycosylated proteins of desmosomes and immunolocalization of a third plaque protein: desmoplakin III.

Expression of unusually large keratins during terminal differentiation: balance of type I and type II keratins is not disrupted.

Structural and Functional Diversity of Desmosomes

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