Journal of the Society for Gynecologic Investigation

 

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Journal of the Society for Gynecologic Investigation, Vol. 2, No. 5, 686-690 (1995)
DOI: 10.1177/107155769500200504

Localization of Fibrillin-I in the Human Term Placenta

Sig-Linda Jacobson, MD

Department of Obstetrics and Gynecology, L-466, Oregon Health Sciences University, 3181 SW Sam Jackson Park Road, Portland, OR 97201

Dwight Kimberly, MS

Kent Thornburg, PhD

Cheryl Maslen, PhD

Departments of Obstetrics and Gynecology, Physiology, Medicine, and Molecular and Medical Genetics; University Congenital heart Research Center, Oregon Health Sciences University Portland; Department of Biology, George Fox College, Newberg, Oregon

Objective: We determined the level of message for fibrillin-1, a single-stranded glycoprotein found in the elastic micropfibrils of the extracellular matrix, in human placenta compared with other adult human tissues and localized the protein int he term human placenta.

Methods: Northern blot analysis using a cDNA specific for fibrillin-1 was used to compare message levels in several adult human tissues and placenta. Immunohistochemical staining, using a monoclonal antibody to human fibrillin-1, was used to visualize the sitz of fibrillin-1 in term human placenta.

Results: Larger amounts of message for fibrillin-1 were present in placenta than in any of the other tissues tested. Staining for fibrillin-1 was present in the villous stroma but not in the basement membranes, trophoblast cells, or in blood vessels of stem, mature intermediate, or terminal villi.

Conclusions: Fibrillin-1 is distributed extensively in the villous stroma of the term human placenta and may contribute elastic properties to the placenta and basal plate required for an active uterus.

Key Words: Placenta • extracellular matix • fibrillin-1 • microfibril • immunohistochemistry


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