A monoclonal antibody to the carboxyterminal domain of procollagen type I visualizes collagen-synthesizing fibroblasts. Detection of an altered fibroblast phenotype in lungs of patients with pulmonary fibrosis.

McDonald, John A.; Broekelmann, T J; Matheke, ML; Crouch, Edmond C.; Koo, Moses; Kuhn, Charles

doi:10.1172/jci112707

Cited by 116 publications

(51 citation statements)

References 30 publications

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“…Other anti-fibroblast antibodies have been found to recognize only proliferating fibroblasts. The 5B5 antibody and the (anti-pC) fibroblast-specific antibody, which recognizes the portion of the procollagen molecule that is cleaved before secretion, recognize only fibroblasts that are actively dividing (McDonald et al 1986;Janin et al 1990). This limits their usefulness for identifying fibroblasts in quiescent conditions.…”

Section: Discussionmentioning

confidence: 99%

An Immunohistochemical Method for Identifying Fibroblasts in Formalin-fixed, Paraffin-embedded Tissue

Goodpaster

Legesse‐Miller

Hameed

et al. 2007

J Histochem Cytochem.

136

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Fibroblasts are critical for tissue homeostasis, and their inappropriate proliferation and activation can result in common and debilitating conditions including fibrosis and cancer. We currently have a poor understanding of the mechanisms that control the growth and activation of fibroblasts in vivo, in part because of a lack of suitable fibroblast markers. We have taken advantage of an antibody previously shown to stain stromal cells in frozen tissues (TE-7) and identified conditions in which it can be used to stain fibroblasts and myofibroblasts in the paraffin-embedded tissue samples routinely collected for pathological analysis. We show that this antibody recognizes growing and quiescent fibroblasts and myofibroblasts by immunohistochemistry, immunofluorescence, and ELISA assays. We also present its staining patterns in normal tissue samples and in breast tumors.

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Section: Discussionmentioning

confidence: 99%

An Immunohistochemical Method for Identifying Fibroblasts in Formalin-fixed, Paraffin-embedded Tissue

Goodpaster

Legesse‐Miller

Hameed

et al. 2007

J Histochem Cytochem.

136

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“…Intra-alveolar fibroblasts are found in proximity to both collagen-and fibronectin-rich areas in IPF, 37 suggesting the possible role of ECM signaling in the pathophysiology of IPF. 38 In fact, integrins, which are receptors of ECM proteins, regulate lung fibroblast migration across the basement membrane in IPF.…”

Section: Discussionmentioning

confidence: 99%

RETRACTED: Discoidin Domain Receptor 1 Contributes to the Survival of Lung Fibroblast in Idiopathic Pulmonary Fibrosis

Matsuyama

Watanabe

Shirahama

et al. 2006

The American Journal of Pathology

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Idiopathic pulmonary fibrosis (IPF), characterized by fibroblast proliferation and accumulation of extracellular matrix, including collagen, is a chronic progressive disorder that results in lung remodeling and fibrosis. However, the cellular mechanisms that may make fibroblasts resistant to apoptosis have not been completely elucidated. Discoidin domain receptor 1 (DDR1), a receptor tyrosine kinase whose ligand is collagen, is expressed in vivo and contributes in vitro to leukocyte differentiation and nuclear factor (NF)-B activation, which may play an important role in fibroblast survival. In this study, we examined in vivo and in vitro DDR1 expression and its role in cell survival using fibroblasts obtained from IPF and non-IPF patients. Immunohistochemically, fibroblasts present in fibroblastic foci expressed endogenous DDR1. The DDR1 expression level was significantly higher in fibroblasts from IPF patients, and the predominant isoform was DDR1b. In IPF patients, DDR1 activation in fibroblasts inhibited Fas ligand-induced apoptosis and resulted in NF-B nuclear translocation. Suppression of DDR1 expression in fibroblasts by siRNA abolished these effects, and an NF-B inhibitor abrogated the anti-apoptotic effect of DDR1 activation. We propose that DDR1 contributes to fibroblast survival in the tissue microenvironment of IPF and that DDR1 up-regulation may occur in other fibroproliferative lung diseases as well. (Am J Pathol

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“…Antibody B3/D6 recognizes chicken plasma and cellular fibronectin (Gardner and Fambrough, 1983); antibody 31-3 recognizes chicken laminin (Bayne et al, 1984). To monitor type I collagen production, we used the M38 antibody which recognizes the carboxyterminal propeptide of type I collagen (McDonald et al, 1986). Rabbit polyclonal antibody to laminin was obtained from Hynda Kleinman (National Institute of Dental Research, Bethesda, MD).…”

Section: Methodsmentioning

confidence: 99%

Expression of β1 integrins changes during transformation of avian lens epithelium to mesenchyme in collagen gels

Żuk

Hay

1994

Developmental Dynamics

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Remarkably, a number of definitive epithelia, such as that of the anterior lens, give rise when suspended within 3D gels of type I collagen, to elongate, bipolar shaped cells that exhibit the ultrastructure, polarity, and migratory ability of mesenchymal cells. They begin producing type I collagen and stop producing crystallins, type IV collagen, and laminin. Here, we investigated changes in p l integrins and their extracellular matrix (ECM) ligands during this transdifferentiation. The former free surface of the lens epithelium that is now in contact with collagen begins within a day to stain intensely for p l and it is this surface rather than the surface facing the basement membranc that gives rise to mesenchyma1 cells. Immunoprecipitation experiments reveal a large increase in the pl integrin subunit on mesenchymal cells as compared to the epithelium of origin. The a 5 integrin subunit, which is barely detectable in the lens, increases in the mesenchyma1 cells and a3 continues to be expressed at about the same level as in the epithelium. 016, the epithelial integrin subunit, and laminin, its ECM ligand, are not detected immunohistochemically or biochemically in the mesenchyme. Rather, the mesenchymal cells secrete abundant fibronectin, the major ECM ligand for a5pl. RGD peptides do not inhibit the transformation but antibodies to p l do perturb the emigration of mesenchymal cells from the lens apical surface. We conclude that the p l integrins newly expressed on the apical epithelial surface interact with the surrounding 3D collagen gel to help bring about this unusual epithelial-mesenchymal transition. o

show abstract

A monoclonal antibody to the carboxyterminal domain of procollagen type I visualizes collagen-synthesizing fibroblasts. Detection of an altered fibroblast phenotype in lungs of patients with pulmonary fibrosis.

Cited by 116 publications

References 30 publications

An Immunohistochemical Method for Identifying Fibroblasts in Formalin-fixed, Paraffin-embedded Tissue

An Immunohistochemical Method for Identifying Fibroblasts in Formalin-fixed, Paraffin-embedded Tissue

RETRACTED: Discoidin Domain Receptor 1 Contributes to the Survival of Lung Fibroblast in Idiopathic Pulmonary Fibrosis

Expression of β1 integrins changes during transformation of avian lens epithelium to mesenchyme in collagen gels

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