TY - JOUR
T1 - Peritrophic matrix of the black fly Simulium vittatum
T2 - Formation, structure, and analysis of its protein components
AU - Ramos, Alfredo
AU - Mahowald, Anthony
AU - Jacobs‐Lorena, Marcelo
PY - 1994/3/15
Y1 - 1994/3/15
N2 - The peritrophic matrix (PM) (same as peritrophic membrane) is secreted by the midgut epithelium of insects and completely surrounds the ingested food. The PM is likely to influence disease transmission by hematophagous insects. As a prelude to a more detailed examination of PM function, we report on morphological and molecular studies of the PM type 1 (PM1) from Simulium vittatum. The blood meal induces major changes in epithelial cell morphology: cells become flattened, microvilli decrease dramatically in number, and organelles redistribute in the cytoplasm. The PM1 forms within minutes of the blood meal. After 6 h the PM1 has reached its maximum thickness (approximately 13 μm) and strength. Two‐dimensional gel electrophoresis reveals two major PM1‐specific proteins of 66 and 61 kDa. Synthesis of these PM1 proteins is likely to be induced by the blood meal, since they are not detectable prior to blood feeding. The time course of accumulation and disappearance of the PM1 proteins closely correlates with the appearance and disappearance of the PM1 itself. © 1994 Wiley‐Liss, Inc.
AB - The peritrophic matrix (PM) (same as peritrophic membrane) is secreted by the midgut epithelium of insects and completely surrounds the ingested food. The PM is likely to influence disease transmission by hematophagous insects. As a prelude to a more detailed examination of PM function, we report on morphological and molecular studies of the PM type 1 (PM1) from Simulium vittatum. The blood meal induces major changes in epithelial cell morphology: cells become flattened, microvilli decrease dramatically in number, and organelles redistribute in the cytoplasm. The PM1 forms within minutes of the blood meal. After 6 h the PM1 has reached its maximum thickness (approximately 13 μm) and strength. Two‐dimensional gel electrophoresis reveals two major PM1‐specific proteins of 66 and 61 kDa. Synthesis of these PM1 proteins is likely to be induced by the blood meal, since they are not detectable prior to blood feeding. The time course of accumulation and disappearance of the PM1 proteins closely correlates with the appearance and disappearance of the PM1 itself. © 1994 Wiley‐Liss, Inc.
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U2 - 10.1002/jez.1402680403
DO - 10.1002/jez.1402680403
M3 - Article
C2 - 8195743
AN - SCOPUS:0028773123
VL - 268
SP - 269
EP - 281
JO - Journal of Experimental Zoology Part A: Comparative Experimental Biology
JF - Journal of Experimental Zoology Part A: Comparative Experimental Biology
SN - 0022-104X
IS - 4
ER -