1994Microscopy Research and TechniqueOpen access

The borderline: Basement membranes and the transition from premalignant to malignant neoplasia

Fred T. Bosman

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Abstract

In this paper, the use of immunohistochemistry for the analysis of basement membrane components and related extracellular matrix proteins in human cancer is reviewed. Basement membranes in cancer are dynamic structures that are constantly degraded but also deposited, in close collaboration between tumor cells and stromal cells. Basement membrane immunohistochemistry, using antibodies against type IV collagen and laminin, appears to be a useful tool in the analysis of lesions on the borderline between premalignant and malignant. Basement membrane interruptions, however, cannot be used as the only criterion for the diagnosis of malignancy. Type VII collagen is often degraded prior to type IV collagen and laminin in early invasion. This protein also tends to be expressed in carcinomas when it is not found in the corresponding normal tissue. Tenascin seems to play a complex role in the development of human tumors, including promotion of cell growth and differentiation, cell migration during invasion, and tissue remodeling during the development of primary and metastatic lesions. Further systemic exploration of extracellular matrix molecules in neoplasms should yield new information relevant for cancer biologists and useful in cancer diagnosis.

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What this paper is about

In this paper, the use of immunohistochemistry for the analysis of basement membrane components and related extracellular matrix proteins in human cancer is reviewed. Basement membranes in cancer are dynamic structures that are constantly degraded but also deposited, in close collaboration between tumor cells and stromal cells. Basement membrane immunohistochemistry, using antibodies against type IV collagen and laminin, appears to be a useful tool in the analysis of lesions on the borderline between premalignant and malignant. Basement membrane interruptions, however, cannot be used as the only criterion for the diagnosis of malignancy. Type VII collagen is often degraded prior to type IV collagen and laminin in early invasion. This protein also tends to be expressed in carcinomas when it is not found in the corresponding normal tissue. Tenascin seems to play a complex role in the development of human tumors, including promotion of cell growth and differentiation, cell migration during invasion, and tissue remodeling during the development of primary and metastatic lesions. Further systemic exploration of extracellular matrix molecules in neoplasms should yield new information relevant for cancer biologists and useful in cancer diagnosis.

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Available abstract

In this paper, the use of immunohistochemistry for the analysis of basement membrane components and related extracellular matrix proteins in human cancer is reviewed. Basement membranes in cancer are dynamic structures that are constantly degraded but also deposited, in close collaboration between tumor cells and stromal cells. Basement membrane immunohistochemistry, using antibodies against type IV collagen and laminin, appears to be a useful tool in the analysis of lesions on the borderline between premalignant and malignant. Basement membrane interruptions, however, cannot be used as the only criterion for the diagnosis of malignancy. Type VII collagen is often degraded prior to type IV collagen and laminin in early invasion. This protein also tends to be expressed in carcinomas when it is not found in the corresponding normal tissue. Tenascin seems to play a complex role in the development of human tumors, including promotion of cell growth and differentiation, cell migration during invasion, and tissue remodeling during the development of primary and metastatic lesions. Further systemic exploration of extracellular matrix molecules in neoplasms should yield new information relevant for cancer biologists and useful in cancer diagnosis.

Key concepts: Basement membrane, Laminin, Tenascin, Extracellular matrix, Pathology, Malignancy, Type IV collagen, Stromal cell

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