Immunolocalization of low-molecular-weight stress protein HSP 27 in normal skin and common cutaneous lesions

Research output: Contribution to journalArticle

49 Citations (Scopus)

Abstract

Stress proteins, which are found ubiquitously in mammalian cells, appear to be implicated in the regulation of cell growth and protection from environmental insult. Although we previously demonstrated the expression of low-molecular-weight stress protein, HSP 27, in cultured keratinocytes, HSP 27 has not yet been identified in human skin. Using standard immunohistochemistry on routinely processed paraffin sections, we examined specimens of common epidermal lesions and normal skin with a monoclonal antibody to HSP 27. Normal skin from the breast, foreskin, and lower extremity demonstrated strong cytoplasmic staining in the suprabasal epidermis. There was no change in the intensity of staining or cellular localization related to age, body location, or gender. Sections of actinic keratosis, superficial basal cell carcinoma, seborrheic keratosis, and psoriasis also exhibited strong cytoplasmic staining in the suprabasal layers of the epidermis. In contrast, cutaneous squamous cell carcinoma demonstrated only weak cytoplasmic staining throughout the infiltrating tumor. This is of particular interest, since other investigators have reported a loss of HSP 27 expression in oncogenically transformed cells that exhibit a tumorigenic phenotype. To our knowledge, this study provides the first demonstration of HSP 27 expression in human skin.

Original languageEnglish (US)
Pages (from-to)504-509
Number of pages6
JournalAmerican Journal of Dermatopathology
Volume16
Issue number5
StatePublished - 1994

Fingerprint

Heat-Shock Proteins
Molecular Weight
Skin
Staining and Labeling
Epidermis
Seborrheic Keratosis
Actinic Keratosis
Foreskin
Cytoprotection
Basal Cell Carcinoma
Keratinocytes
Psoriasis
Paraffin
Squamous Cell Carcinoma
Lower Extremity
Breast
Immunohistochemistry
Monoclonal Antibodies
Research Personnel
Phenotype

Keywords

  • Epidermis
  • Heat shock protein
  • HSP 27
  • srp 27
  • Stress response protein

ASJC Scopus subject areas

  • Dermatology
  • Pathology and Forensic Medicine

Cite this

@article{d630559ba40348ce915522063e6e711c,
title = "Immunolocalization of low-molecular-weight stress protein HSP 27 in normal skin and common cutaneous lesions",
abstract = "Stress proteins, which are found ubiquitously in mammalian cells, appear to be implicated in the regulation of cell growth and protection from environmental insult. Although we previously demonstrated the expression of low-molecular-weight stress protein, HSP 27, in cultured keratinocytes, HSP 27 has not yet been identified in human skin. Using standard immunohistochemistry on routinely processed paraffin sections, we examined specimens of common epidermal lesions and normal skin with a monoclonal antibody to HSP 27. Normal skin from the breast, foreskin, and lower extremity demonstrated strong cytoplasmic staining in the suprabasal epidermis. There was no change in the intensity of staining or cellular localization related to age, body location, or gender. Sections of actinic keratosis, superficial basal cell carcinoma, seborrheic keratosis, and psoriasis also exhibited strong cytoplasmic staining in the suprabasal layers of the epidermis. In contrast, cutaneous squamous cell carcinoma demonstrated only weak cytoplasmic staining throughout the infiltrating tumor. This is of particular interest, since other investigators have reported a loss of HSP 27 expression in oncogenically transformed cells that exhibit a tumorigenic phenotype. To our knowledge, this study provides the first demonstration of HSP 27 expression in human skin.",
keywords = "Epidermis, Heat shock protein, HSP 27, srp 27, Stress response protein",
author = "Gandour-Edwards, {Regina F} and M. McClaren and Isseroff, {Roslyn Rivkah}",
year = "1994",
language = "English (US)",
volume = "16",
pages = "504--509",
journal = "American Journal of Dermatopathology",
issn = "0193-1091",
publisher = "Lippincott Williams and Wilkins",
number = "5",

}

TY - JOUR

T1 - Immunolocalization of low-molecular-weight stress protein HSP 27 in normal skin and common cutaneous lesions

AU - Gandour-Edwards, Regina F

AU - McClaren, M.

AU - Isseroff, Roslyn Rivkah

PY - 1994

Y1 - 1994

N2 - Stress proteins, which are found ubiquitously in mammalian cells, appear to be implicated in the regulation of cell growth and protection from environmental insult. Although we previously demonstrated the expression of low-molecular-weight stress protein, HSP 27, in cultured keratinocytes, HSP 27 has not yet been identified in human skin. Using standard immunohistochemistry on routinely processed paraffin sections, we examined specimens of common epidermal lesions and normal skin with a monoclonal antibody to HSP 27. Normal skin from the breast, foreskin, and lower extremity demonstrated strong cytoplasmic staining in the suprabasal epidermis. There was no change in the intensity of staining or cellular localization related to age, body location, or gender. Sections of actinic keratosis, superficial basal cell carcinoma, seborrheic keratosis, and psoriasis also exhibited strong cytoplasmic staining in the suprabasal layers of the epidermis. In contrast, cutaneous squamous cell carcinoma demonstrated only weak cytoplasmic staining throughout the infiltrating tumor. This is of particular interest, since other investigators have reported a loss of HSP 27 expression in oncogenically transformed cells that exhibit a tumorigenic phenotype. To our knowledge, this study provides the first demonstration of HSP 27 expression in human skin.

AB - Stress proteins, which are found ubiquitously in mammalian cells, appear to be implicated in the regulation of cell growth and protection from environmental insult. Although we previously demonstrated the expression of low-molecular-weight stress protein, HSP 27, in cultured keratinocytes, HSP 27 has not yet been identified in human skin. Using standard immunohistochemistry on routinely processed paraffin sections, we examined specimens of common epidermal lesions and normal skin with a monoclonal antibody to HSP 27. Normal skin from the breast, foreskin, and lower extremity demonstrated strong cytoplasmic staining in the suprabasal epidermis. There was no change in the intensity of staining or cellular localization related to age, body location, or gender. Sections of actinic keratosis, superficial basal cell carcinoma, seborrheic keratosis, and psoriasis also exhibited strong cytoplasmic staining in the suprabasal layers of the epidermis. In contrast, cutaneous squamous cell carcinoma demonstrated only weak cytoplasmic staining throughout the infiltrating tumor. This is of particular interest, since other investigators have reported a loss of HSP 27 expression in oncogenically transformed cells that exhibit a tumorigenic phenotype. To our knowledge, this study provides the first demonstration of HSP 27 expression in human skin.

KW - Epidermis

KW - Heat shock protein

KW - HSP 27

KW - srp 27

KW - Stress response protein

UR - http://www.scopus.com/inward/record.url?scp=0028061833&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028061833&partnerID=8YFLogxK

M3 - Article

VL - 16

SP - 504

EP - 509

JO - American Journal of Dermatopathology

JF - American Journal of Dermatopathology

SN - 0193-1091

IS - 5

ER -