Small proline‐rich protein 1 is the major component of the cell envelope of normal human oral keratinocytes

Lee, Chong Heon; Marekov, Lyuben N.; Kim, Soo-Youl; Brahim, Jaime S.; Park, Myung Hee; Steinert, Peter M.

doi:10.1016/s0014-5793(00)01806-8

Cited by 33 publications

(29 citation statements)

References 28 publications

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“…The high expression of SPRR3 in esophagus and its absence from epidermis (27), as well as the elevated expression of SPRR1 in internal epithelia (48) have previously been observed. An interesting novel observation is the preferential expression of SPRR2G and SPRR4 in skin.…”

Section: Discussionmentioning

confidence: 53%

Structural Organization and Regulation of the Small Proline-rich Family of Cornified Envelope Precursors Suggest a Role in Adaptive Barrier Function

Cabral

Voskamp

Cleton‐Jansen

et al. 2001

Journal of Biological Chemistry

154

145

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The protective barrier provided by stratified squamous epithelia relies on the cornified cell envelope (CE), a structure synthesized at late stages of keratinocyte differentiation. It is composed of structural proteins, including involucrin, loricrin, and the small proline-rich (SPRR) proteins, all encoded by genes localized at human chromosome 1q21. The genetic characterization of the SPRR locus reveals that the various members of this multigene family can be classified into two distinct groups with separate evolutionary histories. Whereas group 1 genes have diverged in protein structure and are composed of three different classes (SPRR1 (2؋), SPRR3, and SPRR4), an active process of gene conversion has counteracted diversification of the protein sequences of group 2 genes (SPRR2 class, seven genes). Contrasting with this homogenization process, all individual members of the SPRR gene family show specific in vivo and in vitro expression patterns and react selectively to UV irradiation. Apparently, creation of regulatory rather than structural diversity has been the driving force behind the evolution of the SPRR gene family. Differential regulation of highly homologous genes underlines the importance of SPRR protein dosage in providing optimal barrier function to different epithelia, while allowing adaptation to diverse external insults.

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Section: Discussionmentioning

confidence: 53%

Structural Organization and Regulation of the Small Proline-rich Family of Cornified Envelope Precursors Suggest a Role in Adaptive Barrier Function

Cabral

Voskamp

Cleton‐Jansen

et al. 2001

Journal of Biological Chemistry

154

145

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“…Interestingly, the components of the CE vary in different epithelia and body sites. Loricrin comprises the major component (70%) of the CE in interfollicular cutaneous keratinocytes (13,14), whereas SPR1 is the major component of the CE in human oral keratinocytes (15).…”

mentioning

confidence: 99%

Molecular Cloning and Expression of Keratinocyte Proline-rich Protein, a Novel Squamous Epithelial Marker Isolated During Skin Development

Kong

Longaker

Lorenz

2003

Journal of Biological Chemistry

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We describe a novel rat cDNA named keratinocyte proline-rich protein (KPRP) isolated by RNA differential display during skin development. We determine that KPRP is expressed in stratified squamous epithelium, and its ϳ2.8-kb cDNA encodes a 699-amino acid protein with high proline content (19%). KPRP is an insoluble protein, similar to most epidermal terminal differentiation-associated proteins. Immunoblot of the protein lysate from keratinocytes, using strong reducing conditions, demonstrates two KPRP bands of ϳ76 and 55 kDa size. KPRP is expressed in stratified squamous epithelia of skin, tongue, and esophagus. The initiation of KPRP expression in fetal rat skin at E17, E18, E19, E20, and E21 was analyzed by reverse transcription-PCR. Fetal skin at E19 and later expresses KPRP. In situ hybridization of skin from E18, E19, and 4-day-old neonatal rats demonstrates that interfollicular and follicular keratinocytes express KPRP. Anti-KPRP antibody demonstrates KPRP protein localizes to all layers of stratified epithelia in skin, tongue, and esophagus. In cultured dermal keratinocytes, KPRP is diffusely distributed throughout the cytoplasm with denser staining adjacent to the nuclear and plasma membranes. Additionally, immunoreactive intracellular granules are observed during keratinocyte detachment from their plastic substrate. Rat KPRP has 89% homology to a mouse genomic DNA sequence and 56% homology to a human hypothetical protein. We conclude that KPRP may be a new epidermal terminal differentiation-related protein expressed in stratified squamous epithelia. KPRP is expressed by fetal dermal keratinocytes during late gestation and is a new marker of maturing epidermis during fetal skin development.The epithelial layer of the skin provides an essential function as a protective barrier against insult from the outside environment. Although the adaptive barrier function of the epidermis begins during skin development, it is maintained after birth by the terminal differentiation process in the epidermis. Epidermal terminal differentiation genes have been well studied during the last decade, and at least 32 genes from three related families have been identified (1). The three terminal differentiation-related families are the cornified cell envelope (CE) 1 proteins, the keratin intermediate filament-associated proteins, and some calcium-binding proteins (2-5). These genes are clustered, have evolutionarily conserved structure, and are located on chromosome 1q21 in humans (6, 7) chromosome 3 in mice (8), and as we have determined for this study, chromosome 2 in rats. Additionally, the CE proteins have an ordered expression during fetal skin development. In humans, epidermal expression of involucrin begins at 14 weeks gestation when periderm is present. Loricrin and the small proline-rich proteins (SPRs) expression begins at 16 weeks when the epidermis is immature but already developing into a multilayered structure. Filaggrin and trichohyalin expression starts at 24 weeks, which is a developmental stage when the fetal s...

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“…The FGF family also serve an important role in fibroblast growth (31). Meanwhile, Lee et al (32) reported that …”

Section: Discussionmentioning

confidence: 99%

Gene expression profiling and bioinformatics analysis of hereditary gingival fibromatosis

Fang

Wang²,

Chen

2017

biom rep

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Abstract. Hereditary gingival fibromatosis (HGF) is a benign, non-hemorrhagic and fibrous gingival overgrowth that may cover all or part of the teeth. It typically interferes with speech, lip closure and chewing, and can also be a psychological burden that affects the self-esteem of patients. Owing to high genetic heterogeneity, genetic testing to confirm diagnosis is not justified. It is therefore important to identify key signature genes and to understand the molecular mechanisms underlying HGF. The aim of the present study was to determine HGF-related genes and to analyze these genes through bioinformatics methods. A total of 249 differentially expressed genes (DEGs), consisting of 65 upregulated and 184 downregulated genes, were identified in the GSE4250 dataset of Gene Expression Omnibus (GEO) when comparing with the gums of HGF patients with those of healthy controls using the affy and limma packages in R. Subsequently, 28 enriched gene ontology terms were obtained from the Database for Annotation, Visualization and Integrated Discovery, and a protein-protein interaction (PPI) network was constructed and analyzed using STRING and Cytoscape. There were 99 nodes and 118 edges in the PPI network of these DEGs obtained through STRING. Among these nodes, 12 core genes were identified, of which the highest degree node was the gene for POTE ankyrin domain family member I. Collectively the results indicate that bioinformatics methods may provide effective strategies for predicting HGF-related genes and for understanding the molecular mechanisms of HGF.

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Small proline‐rich protein 1 is the major component of the cell envelope of normal human oral keratinocytes

Cited by 33 publications

References 28 publications

Structural Organization and Regulation of the Small Proline-rich Family of Cornified Envelope Precursors Suggest a Role in Adaptive Barrier Function

Structural Organization and Regulation of the Small Proline-rich Family of Cornified Envelope Precursors Suggest a Role in Adaptive Barrier Function

Molecular Cloning and Expression of Keratinocyte Proline-rich Protein, a Novel Squamous Epithelial Marker Isolated During Skin Development

Gene expression profiling and bioinformatics analysis of hereditary gingival fibromatosis

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