Hostname: page-component-84b7d79bbc-g7rbq Total loading time: 0 Render date: 2024-07-27T22:22:36.881Z Has data issue: false hasContentIssue false

Association of a Brush Border Myosin I-Like Protein with Vesicular Organelles of the Secretory Pathway in Chicken Enterocytes

Published online by Cambridge University Press:  02 July 2020

László G. Kömüves
Affiliation:
University of California San Francisco, VA Medical Center, San Francisco, CA, 94121
Scott Munson
Affiliation:
University of California San Francisco, VA Medical Center, San Francisco, CA, 94121
Daniel D. Bikle
Affiliation:
University of California San Francisco, VA Medical Center, San Francisco, CA, 94121
Get access

Extract

Brush border myosin I (BBMI) was first identified as a major constituent of the microvillus cytoskeleton, where it links the actin filaments of the microvillus core to the overlying plasma membrane. Recently, however, BBMI was also found on isolated Golgi membranes. This observation suggests that cytoplasmic BBMI might act as a molecular motor for apically targeted secretory vesicles.

In an earlier study from this laboratory a 105-110 kD protein was isolated from the chicken small intestine, which displayed several characteristics of the BBMI. Using an antibody against this BBMI- like protein (MLP), the protein was detected in the apical brush border of the enterocytes. The limited resolution of the light microscopic immunohistochemical techniques used in that investigation, however, did not provide information about the intracellular distribution of MLP in the enterocytes.

In this study the intracellular localization of MLP was characterized using post-embedding colloidal gold immunocytochemistry. Pieces of the jejunum from 6-week-old male White Leghorn chickens were fixed and embedded in LR Gold resin.

Type
Imaging Cells and Organelles
Copyright
Copyright © Microscopy Society of America 1997

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

1.Mooseker, M. S. and Cheney, R. E., Ann Rev. Cell Biol, 11 ( 1996) 633.10.1146/annurev.cb.11.110195.003221CrossRefGoogle Scholar
2.Fath, K. R., Timbur, G. M. and Burgess, D. R., J. Cell Biol., 126 (1994) 661.10.1083/jcb.126.3.661CrossRefGoogle Scholar
3.Bikle, D. D., Munson, S. and Mancianti, M.-L., Gastroenterology, 100 (1991) 395.10.1016/0016-5085(91)90208-3CrossRefGoogle Scholar
4.Kömüves, L. G. and Heath, J. P., J. Histochem. Cytochem., 40 (1992) 1637.10.1177/40.11.1431052CrossRefGoogle Scholar
5.Bikle, D. D., Munson, S. and Kömüves, L. G., J. Biol. Chem., 271 (1996) 9075.10.1074/jbc.271.15.9075CrossRefGoogle Scholar