Microvilli are observed on the plasma surface of eggs, aiding in the anchoring of sperm cells that have penetrated the extracellular coat of egg cells. Clustering of elongated microtubules around a sperm allows for it to be drawn closer and held firmly so fusion can occur.
Microvilli are also of importance on the cell surface of white blood cells, as they aid in the migration of white blood cells.
Each microvillus has a dense bundle of cross-linked actin filaments, which serves as its structural core. 20 to 30 tightly bundled actin filaments are cross-linked by bundling proteins fimbrin and villin to form the core of the microvilli.
In the enterocyte microvillus, the structural core is attached to the plasma membrane along its length by lateral arms made of myosin Ia and Ca2+ binding protein calmodulin. Myosin Ia functions through a binding site for filamentous actin on one end and a lipid binding domain on the other. The plus ends of the actin filaments are located at the tip of the microvillus, while the minus ends are anchored in the ‘terminal web’ composed of a complicated set of proteins including spectrin and myosin II.
Actin filaments, present in the cytosol, are most abundant near the cell surface. These filaments are thought to determine the shape and movement of the plasma membrane.
The nucleation of actin fibers occurs as a response to external stimuli, allowing a cell to alter its shape to suit a particular situation.
This could account for the uniformity of the microvilli, which are observed to be of equal length and diameter. This nucleation process occurs from the minus end, allowing rapid growth from the plus end.
Interestingly, though the length and composition of microvilli is consistent within a certain group of homogenous cells, it can differ slightly in a different part of the same organism.
For example, the microvilli in the small and large intestines in mice are slightly different in length and amount of surface coat covering.
This layer may be used to aid binding of substances needed for uptake, to adhere nutrients or as protection against harmful elements.
It can be another location for functional enzymes to be localized.
This is seen in infections caused by EPEC subgroup Escherichia coli, in Celiac disease, and Microvillus Inclusion Disease (an inherited disease characterized by defective microvilli and presence of cytoplasmic inclusions of the cell membrane other than the apical surface).
The destruction of microvilli can actually be beneficial sometimes, as in the case of elimination of microvilli on white blood cells which can be used to combat auto immune diseases.
Congenital lack of microvilli in the intestinal tract causes microvillous atrophy, a rare, usually fatal condition found in new-born babies.
Comparison of PSGL-1 microbead and neutrophil rolling: Microvillus elongation stabilizes P-selectin bond clusters
Apr 01, 2002; ABSTRACT A cell-scaled microbead system was used to analyze the force-dependent kinetics of P-selectin adhesive bonds independent...