The S-100 Protein Family: A Biochemical and Functional Overview

Hilt, Dana; Kligman, Douglas

doi:10.1007/978-3-642-76150-8_6

Cited by 86 publications

(84 citation statements)

References 107 publications

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“…The S100 proteins are a family of small, acidic, Ca 2ϩ -binding proteins that contain two Ca 2ϩ -binding EF hands (67,68). S100 proteins are thought to function like calmodulin, having an important role in calcium-dependent signaling (67,68).…”

Section: Discussionmentioning

confidence: 99%

“…It is thought that binding of calcium to the EF hands of the S100 proteins results in a conformation change that exposes protein-interaction sites (68). The activated S100 proteins then bind to and regulate the function of target proteins (67,68). Many of the S100 genes, including S100A10 (69, 70) and S100A11 (54,71), have been co-localized on the same chromosome as other epidermal structural protein genes, suggesting a possible function in skin.…”

Section: Discussionmentioning

confidence: 99%

“…S100A11 interacts with annexin I (76, 77) in a calcium-dependent manner, an interaction that requires the first 12 amino acids of the annexin I amino terminus (77). The central hinge and carboxyl terminus are the least conserved regions among S100 proteins and are likely to provide the sites that non-covalently bind other proteins (68). It has been suggested (77) that the COOH-terminal segment is not required for the interaction, implicating the hinge region as the annexin I interaction site.…”

Section: Discussionmentioning

confidence: 99%

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S100A11, S100A10, Annexin I, Desmosomal Proteins, Small Proline-rich Proteins, Plasminogen Activator Inhibitor-2, and Involucrin Are Components of the Cornified Envelope of Cultured Human Epidermal Keratinocytes

Robinson

Lapic

Welter

et al. 1997

Journal of Biological Chemistry

205

197

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The cornified envelope (CE) is an insoluble sheath of ⑀-(␥-glutamyl)lysine cross-linked protein, which is deposited beneath the plasma membrane during keratinocyte terminal differentiation. We have probed the structure of the CE by proteolytic cleavage of purified CE fragments isolated from CEs formed spontaneously in cell culture. CNBr digestion, followed by trypsin and then proteinase K treatment released 25%, 42%, and 18%, respectively, of the CE protein. Purification and sequencing of released peptides has identified two novel CE precursors, S100A11 (S100C, calgizzarin) and S100A10 (calpactin light chain). We also sequenced peptides derived from annexin I and plasminogen activator inhibitor 2, two putative envelope precursors, as well as portions of the well established CE precursor proteins SPR1A, SPR1B, and involucrin. Many desmosomal components were identified (desmoglein 3, desmocolin A/B, desmoplakin I, plakoglobin, and plakophilin), indicating that desmosomes become cross-linked into the CE. Fragments derived from envoplakin, the recently sequenced 210-kDa membranous CE precursor protein, which also appears to be a desmosomal component, were also identified. Analysis of the pattern of peptide release following the sequential digestion indicates that S100A11 is anchored to the envelope via Gln 102 and/or Lys 103 at the carboxyl terminus and at Lys 3 , Lys 23 , and/or Gln 22 in the amino terminus. A similar type of analysis indicates that small proline-rich proteins 1A and 1B (SPR1A and SPR1B) become cross-linked at the amino terminus (residues 1-23) and the carboxyl terminus (residues 86 -89). No loricrin, cystatin A, or elafin peptides were detected.The cornified cell envelope (CE) 1 is a 15-nm-thick crosslinked sheath of protein that forms beneath the plasma membrane during the final stages of epidermal keratinocyte differentiation (1-3). Transglutaminase enzymes catalyze the assembly of this structure via formation of ⑀-(␥-glutamyl)lysine bonds between envelope precursors (4 -7). The proteins that have been identified as constituents of the CE include loricrin (8 -10), involucrin (11-14), the small proline-rich (SPR) family of proteins (15-18), cystatin A (19, 20), elafin (21-23), filaggrin (24 -26), keratin (27, 28), desmosomal components (27), annexin I (29 -31), plasminogen activator inhibitor-2 (PAI-2) (32), and the 195-kDa and 210-kDa proteins (33, 34). Cross-links have been identified within loricrin, elafin, filaggrin, keratin, SPR1, SPR2, and desmoplakin (35). Loricrin is present as a partner in most of these cross-links. It has been proposed that envelope formation is initiated with formation of an envelope scaffolding that consists of soluble precursors, and that other precursors (both soluble and insoluble) are later deposited (3,11,35). The scaffolding has been proposed to consist of involucrin, cystatin A, and possibly other proteins (25). In this model, other proteins, including loricrin, elafin, and SPRs, are deposited onto this scaffolding.In the present report, we study the compositi...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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S100A11, S100A10, Annexin I, Desmosomal Proteins, Small Proline-rich Proteins, Plasminogen Activator Inhibitor-2, and Involucrin Are Components of the Cornified Envelope of Cultured Human Epidermal Keratinocytes

Robinson

Lapic

Welter

et al. 1997

Journal of Biological Chemistry

205

197

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“…We recently identified two S100 proteins, S100A11 (S100C, calgizzarin) and S100A10 (calpactin light chain, p11), as components of cornified envelopes prepared from cultured keratinocytes (7). S100 proteins are thought to be regulators of cell signaling, cell proliferation, and cell structure (8,9). They comprise a family of 10 -12-kilodalton acidic proteins that form homo-and heterodimers and bind calcium via two "EF hand motifs."…”

mentioning

confidence: 99%

Identification of Transglutaminase-reactive Residues in S100A11

Robinson¹,

Eckert²

1998

Journal of Biological Chemistry

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The recent finding that S100A11 is a component of the keratinocyte cornified envelope (CE) (Robinson, N. A., Lapic, S., Welter, J. F., and Eckert, R. L. (1997) J. Biol. Chem. 272, 12035-12046) suggests that S100A11 is a transglutaminase (TG) substrate. In the present study we show that S100A11 forms multimers when cultured keratinocytes are challenged by increased levels of intracellular calcium and that multimer formation is inhibited by the TG inhibitor, cystamine. These S100A11 multimers appear to be incorporated into the CE, as immunoreactive S100A11 is detected in purified envelopes prepared from cultured cells and from foreskin epidermis. To study S100A11 as a transglutaminase substrate, recombinant human S100A11 (rhS100A11) was used in a cell-free cross-linking system.

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“…Contrary to calmodulin, the expression of S100 proteins is cell-and tissue-specific. A wide range of different human diseases has been associated with deregulated expression of S100 genes (1,7,14). S100 proteins have been implicated in pleiotropic cellular events, with specific functions for each of the family members, such as cell cycle regulation, cell growth, cell differentiation, and motility.…”

mentioning

confidence: 99%