Developmental pattern of calmodulin-binding proteins in rat jejunal epithelial cells

Rochette‐Egly, Cécile; Haffen, K

doi:10.1111/j.1432-0436.1987.tb00172.x

Cited by 17 publications

(7 citation statements)

References 41 publications

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“…21 and those composed of the keratin 8/18 pair may participate in the organization of the apical cytoplasmic network, or play some other significant role(s) in the intestinal epithelial cells. At the same time in the rat, and at comparable stages of development in chicks and mice, other important cytoskeletal proteins (such as villin, brush border myosin I, spectrin, caldesmon and TW 260/240) have been found to appear, or to undergo significant changes in cellular distribution [13][14][15][16]55,56]. At the time of birth, or shortly thereafter, the pattern of keratins expressed by the intestinal epithelial cells became similar, or identical, to that observed in adult animals.…”

Section: Discussionmentioning

confidence: 99%

Changes in keratin expression during fetal and postnatal development of intestinal epithelial cells

Calnek

Quaroni

1992

Biochemical Journal

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We have investigated keratin expression in fetal, newborn and adult rat intestines by immunofluorescence staining, immunoblotting of two-dimensional gels and Northern blot analysis of total cellular RNAs. Keratin-type intermediate filaments, composed predominantly of keratin no. 19, were observed already in the undifferentiated stratified epithelium present at 15-16 days of gestation. The marked maturation and differentiation of the epithelium taking place at 18-19 days of gestation was characterized by the appearance of the differentiation-specific keratin no. 21 and by a significant increase in the relative amount of keratin no. 8. The keratin pattern typical of adult villus cells became established at the time of birth, and was marked by a considerable increase in the complexity of the keratin-related polypeptides detected on two-dimensional gels, indicative of extensive post-translational modification of all keratins. Starting at 20 days of gestation there was a major increase in the relative abundance of mRNAs coding for keratin nos. 8, 19 and 21; in contrast, the relative amount of keratin no. 18 mRNA reached a peak shortly after birth and declined to very low levels in adult intestine. These results demonstrated marked changes in keratin expression and post-translational processing taking place at key stages of intestinal development. The appearance of keratin no. 21 in coincidence with the formation of an adult-type brush border and terminal web would be consistent with it having an important role in the organization of the intermediate filament network in the apical cytoplasm of the differentiated intestinal cells.

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Section: Discussionmentioning

confidence: 99%

Changes in keratin expression during fetal and postnatal development of intestinal epithelial cells

Calnek

Quaroni

1992

Biochemical Journal

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“…Thus, it is still critical to verify that the MIHC protein is the ll0-kD subunit of bovine ll0K-CM and not another, as yet uncharacterized, myosin I-like protein found in intestinal tissue. This is an important open question because recent studies by Rochette-Egly and Haffen (1987), using a polyclonal antiserum generated in our laboratory against avian ll0K (for characterization see Shibayama et al, 1987) identified two immunoreactive polypeptides in developing rat intestine: a ll0-kD form and a slightly higher molecular mass form of 130 kD that disappears at birth. Similarly, we (Peterson, Carboni, West, and Mooseker, unpublished observations) have observed both 110-and 120-130-kD immunoreactive forms in preparations of isolated BBs from human ileum and colon.…”

Section: Discussionmentioning

confidence: 99%

Structural and immunological characterization of the myosin-like 110-kD subunit of the intestinal microvillar 110K-calmodulin complex: evidence for discrete myosin head and calmodulin-binding domains.

Carboni

Conzelman

Adams

et al. 1988

The Journal of Cell Biology

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Abstract. The actin bundle within each microvillus of the intestinal brush border is tethered laterally to the membrane by spirally arranged bridges. These bridges are thought to be composed of a protein complex consisting of a llO-kD subunit and multiple molecules of bound calmodulin (CM). Recent studies indicate that this complex, termed l l0K-CM, is myosin-like with respect to its actin binding and ATPase properties. In this study, possible structural similarity between the l l0-kD subunit and myosin was examined using two sets of mAbs; one was generated against Acanthamoeba myosin II and the other against the ll0-kD subunit of avian ll0K-CM. The myosin II mAbs had been shown previously to be cross-reactive with skeletal muscle myosin, with the epitope(s) localized to the 50-kD tryptic fragment of the subfragment-1 (St) domain. The ll0K mAbs (CX 1-5) reacted with the ll0-kD subunit as well as with the heavy chain of skeletal but not with that of smooth or brush border myosin. All five of these ll0K mAbs reacted with the 25-kD, NH2-terminal tryptic fragment of chicken skeletal St, which contains the ATP-binding site of myosin. Similar tryptic digestion of ll0K-CM revealed that these five mAbs all reacted with a 36-kD fragment of ll0K (as well as larger 90-and 54-kD fragments) which by photoaffinity labeling was shown to contain the ATPbinding site(s) of the ll0K subunit. CM binding to these same tryptic digests of ll0K-CM revealed that only the 90-kD fragment retained both ATP-and CMbinding domains. CM binding was observed to several tryptic fragments of 60, 40, 29, and 18 kD, none of which contain the myosin head epitopes. These results suggest structural similarity between the ll0K and myosin St, including those domains involved in ATP-and actin binding, and provide additional evidence that ll0K-CM is a myosin. These studies also support the results of Coluccio and Bretscher (1988. J. Cell Biol. 106:367-373) that the calmodulin-binding site(s) and the myosin head region of the ll0-kD subunit lie in discrete functional domains of the molecule.

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“…Early research on BB cytoskeleton formation focused on embryonic chickens, mice and rats (Chambers and Grey, 1979;Ezzell et al, 1989;Maunoury et al, 1988;Rochette and Haffen, 1987;Shibayama et al, 1987;Stidwill and Burgess, 1986;Takemura et al, 1988), with subsequent work utilizing cell lines (Dudouet et al, 1987;Peterson et al, 1992). Recently, attention has turned to understanding the development of the BB in adult tissues.…”

Section: Brush B O R D Er a S S E M B L Y In In Te S Tin A L C R Yptsmentioning

confidence: 99%

The cytoskeleton in development of epithelial cell polarity

Fath

Mamajiwalla

Burgess

1993

Journal of Cell Science

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SUMMARYThe polarization of intestinal epithelial cells and the stereotypic arrangement of their actin-based cytoskel eton have made these epithelia an excellent system to explore the organization and formation of a cortical actin-based cytoskeleton. Through a combined morpho logical and biochemical analysis, the molecular arrange ment of many of the components of the brush border has been elucidated. Study of brush border assembly in the Crypts of Lieberkiihn suggests that cytoskeletal mRNA and protein expression, as well as morphologi cal development, occur rapidly following cell differen tiation. Protein kinases appear to be important regula tors of intestinal cell growth, for differentiating cells in the crypts possess 15-fold higher levels of tyrosine phosphorylated proteins than differentiated cells of the villus. One of these kinases, pp60c'5Te, has a 4-to 7-fold higher activity in crypts and increased association with the cytoskeleton than it has in villus cells.The development and maintenance of polarization in epithelial cells require the targeting and transport of specific proteins to the apical and basolateral plasma membrane. It has been proposed that a dynein-like, microtubule-based motor is involved in the transport of apically directed materials from the tram-Golgi to the apical plasma membrane. However, microtubules do not reach the plasma membrane, but terminate below the actin-rich network of filaments comprising the terminal web. We propose that vesicles translocate from the Golgi to the apical cytoplasm along microtubules using dynein, and then move through the terminal web to reach the apical plasma membrane using the actin-based motor myosin-I. Our isolation of Golgi-derived vesicles pos sessing both myosin-I and dynein on their cytoplasmic surface is consistent with this hypothesis.

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Developmental pattern of calmodulin-binding proteins in rat jejunal epithelial cells

Cited by 17 publications

References 41 publications

Changes in keratin expression during fetal and postnatal development of intestinal epithelial cells

Changes in keratin expression during fetal and postnatal development of intestinal epithelial cells

Structural and immunological characterization of the myosin-like 110-kD subunit of the intestinal microvillar 110K-calmodulin complex: evidence for discrete myosin head and calmodulin-binding domains.

The cytoskeleton in development of epithelial cell polarity

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