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Retention of nonhelical procollagen containing cis-hydroxyproline in rough endoplasmic reticulum.
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Fibroblasts freshly isolated from embryonic tendons were incubated with a proline analog, cis-4-hydroxy-L-proline, which is incorporated into protein and which leads to the intracellular accumulation of nonhelical procollagen. Evidence is presented here that the nonhelical procollagen containing the
A substrate preference for the rough endoplasmic reticulum resident protein FKBP22 during collagen biosynthesis.
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The biosynthesis of collagens occurs in the rough endoplasmic reticulum and requires a large numbers of molecular chaperones, foldases, and post-translational modification enzymes. Collagens contain a large number of proline residues that are post-translationally modified to 3-hydroxyproline or
Ziploc-ing the structure: Triple helix formation is coordinated by rough endoplasmic reticulum resident PPIases.
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BACKGROUND
Protein folding is crucial for proteins' specific functions and is facilitated by various types of enzymes and molecular chaperones. The peptidyl prolyl cis/trans isomerases (PPIase) are one of these families of enzymes. They ubiquitously exist inside the cell and there are eight PPIases
Rough energy landscapes in protein folding: dimeric E. coli Trp repressor folds through three parallel channels.
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The folding mechanism of the dimeric Escherichia coli Trp repressor (TR) is a kinetically complex process that involves three distinguishable stages of development. Following the formation of a partially folded, monomeric ensemble of species, within 5 ms, folding to the native dimer is controlled by
Efficient sampling over rough energy landscapes with high barriers: A combination of metadynamics with integrated tempering sampling.
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In order to efficiently overcome high free energy barriers embedded in a complex energy landscape and calculate overall thermodynamics properties using molecular dynamics simulations, we developed and implemented a sampling strategy by combining the metadynamics with (selective) integrated tempering
Radioautographic characterization of successive compartments along the rough endoplasmic reticulum-Golgi pathway of collagen precursors in foot pad fibroblasts of [3H]proline-injected rats.
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Young rats given an intravenous injection of [3H]proline were killed at successive times from 4 to 80 min later. Fibroblasts from the front foot pad were radioautographed ; silver grains were counted over several of the organelles and the results were expressed as percent radiolabel per unit volume.
Appearance of dense granules in the rough endoplasmic reticulum of the juxtaglomerular cells in mice administered with captopril.
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Captopril [1-(D-3-mercapto-2-methyl-1-oxopropyl)-L-proline (S,S)] is now known to be an inhibitor of angiotensin-converting enzyme. In male mice, the juxtaglomerular cells were examined by electron microscopy 42 h after administration of captopril. Numerous dense granules appeared in the rough
Rough wave-like heaped overburden promotes establishment of woody vegetation while leveling promotes grasses during unassisted post mining site development.
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Geodiversity plays an important role in species establishment during spontaneous succession. At post-mining sites in the Czech Republic in 2003, we established plots in which the surface of the heaped overburden was either kept wave-like or leveled. Based on surveys conducted from 2006 to 2015,
Rough endoplasmic reticulum trafficking errors by different classes of mutant dentin sialophosphoprotein (DSPP) cause dominant negative effects in both dentinogenesis imperfecta and dentin dysplasia by entrapping normal DSPP.
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Families with nonsyndromic dentinogenesis imperfecta (DGI) and the milder, dentin dysplasia (DD), have mutations in one allele of the dentin sialophosphoprotein (DSPP) gene. Because loss of a single Dspp allele in mice (and likely, humans) causes no dental phenotype, the mechanism(s) underling the
The secretion of collagen by insects: uptake of [3H]proline by collagen-synthesizing cells in Locusta migratoria and Galleria mellonella.
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The uptake of [H3]proline by collagen-secreting cells of the locust, Locusta migratoria, and wax-moth, Galleria mellonella, has been investigated by electron autoradiography. The locust cells are around the ejaculatory duct and they secrete collagen in the young adult male, while the wax-moth cells
Prolactin-induced stimulation of H(3)-proline incorporation into the basement lamella of tadpole skin: light and electron microscope study.
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Radioautographic studies revealed that prolactin markedly stimulates the incorporation of H(3)-proline into the basement lamella of the tail fin of frog tadpole. Radioactivity in fibroblasts reached a peak at 3 hours. Thereafter, the number of silver grains in fibroblasts was reduced with
The effect of colcemid on the structure and secretory activity of ameloblasts in the rat incisor as shown by radioautography after injection of 3H-proline.
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Enamel secretion by ameloblasts was investigated in the incisors of 100 gm normal and colcemid-injected male rats. Morphological studies were done on rats given a single intraperitoneal injection of 0.1 mg (1.25 mM) of colcemid and sacrified 1 to 4 hours after injection. Protein synthesis and
Biochemical and ultrastructural study of the effects of proline analogues on collagen synthesis in 3T6 fibroblasts.
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The effects of proline analogues, L-3,4-dehydroproline and L-azetidine-2-carboxylic acid, on collagen synthesis by cultured 3T6 fibroblasts have been studied. Prolyl hydroxylase activity was partially inhibited in cells cultured with dehydroproline for 24 h, resulting in the synthesis of collagen in
Electron microscopic immunocytochemical localization of proline-rich proteins in normal mouse parotid salivary glands.
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Rabbit polyclonal antibodies against isoproterenol-induced mouse proline-rich proteins (PRPs) were used to localize PRPs in the parotid salivary glands of normal adult BALB/c mice. The antibodies recognized both acidic-type and basic-type PRPs. Immunoblotting experiments revealed that the glands
Differences between proline and lysine hydroxylations in their inhibition by zinc or by ascorbate deficiency during collagen synthesis in various cell types.
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The addition of Zn2+ inhibited lysine hydroxylation markedly less effectively than it did proline hydroxylation in chick embryo tendon cells, 3T6 fibroblasts and lysyl hydroxylase-deficient Ehlers-Danlos Syndrome Type VI fibroblasts. With low Zn2+ concentrations, a similar difference was also seen
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