scholarly journals Human collagen genes encoding basement membrane alpha 1 (IV) and alpha 2 (IV) chains map to the distal long arm of chromosome 13.

1987 ◽  
Vol 84 (2) ◽  
pp. 512-516 ◽  
Author(s):  
C. A. Griffin ◽  
B. S. Emanuel ◽  
J. R. Hansen ◽  
W. K. Cavenee ◽  
J. C. Myers
Keyword(s):  
Basement Membrane ◽  
Chromosome 13 ◽  
Genes Encoding ◽  
Human Collagen ◽  
Collagen Genes

scholarly journals Clinic Case of Rare Type VI Osteogenesis Imperfecta

2019 ◽  
Vol 16 (1) ◽  
pp. 30-35
Author(s):  
Olga N. Ignatovich ◽  
Leyla S. Namazova-Baranova ◽  
Tea V. Margieva ◽  
Natalia V. Zhurkova ◽  
Kirill V. Savostyanov ◽  
...  
Keyword(s):  
Osteogenesis Imperfecta ◽  
High Frequency ◽  
Heterogeneous Group ◽  
Osteogenesis Imperfecta Type ◽  
Post Translational Modification ◽  
Rare Type ◽  
Genes Encoding ◽  
Long Time ◽  
Collagen Genes

Osteogenesis imperfect is genetically heterogeneous group of diseases which are characterized by bone brittleness and fractures. It was thought for a long time that this is happening due to mutations in collagen genes. However, within past decade the understanding of osteogenesis imperfecta etiology has changed as a result of genetics development. The majority of all cases is related to mutations in collagen genes whereas rare mostly recessive forms are related to mutations in genes encoding collagen post-translational modification. Mutations in SERPINF1 gene were chosen as molecular cause of osteogenesis imperfecta type VI in 2011. Thus the new pathophysiology of this disease was revealed. Children with osteogenesis imperfecta type VI have high-frequency of fractures despite the management with bisphosphonates because mineralized bone osteoid is considerably reduced.

Regulation of collagen I gene expression by ras

1992 ◽  
Vol 12 (10) ◽  
pp. 4714-4723
Author(s):  
J L Slack ◽  
M I Parker ◽  
V R Robinson ◽  
P Bornstein
Keyword(s):  
Type I Collagen ◽  
The Body ◽  
Transformed Cells ◽  
Type I ◽  
Mrna Levels ◽  
Oncogenic Ras ◽  
Genes Encoding ◽  
Flanking Region ◽  
Collagen Genes ◽  
I Gene

Although transformation of rodent fibroblasts can lead to dramatic changes in expression of extracellular matrix genes, the molecular basis and physiological significance of these changes remain poorly understood. In this study, we have investigated the mechanism(s) by which ras affects expression of the genes encoding type I collagen. Levels of both alpha 1(I) and alpha 2(I) collagen mRNAs were markedly reduced in Rat 1 fibroblasts overexpressing either the N-rasLys-61 or the Ha-rasVal-12 oncogene. In fibroblasts conditionally transformed with N-rasLys-61, alpha 1(I) transcript levels began to decline within 8 h of ras induction and reached 1 to 5% of control levels after 96 h. In contrast, overexpression of normal ras p21 had no effect on alpha 1(I) or alpha 2(I) mRNA levels. Nuclear run-on experiments demonstrated that the transcription rates of both the alpha 1(I) and alpha 2(I) genes were significantly reduced in ras-transformed cells compared with those in parental cells. In addition, the alpha 1(I) transcript was less stable in transformed cells. Chimeric plasmids containing up to 3.6 kb of alpha 1(I) 5'-flanking DNA and up to 2.3 kb of the 3'-flanking region were expressed at equivalent levels in both normal and ras-transformed fibroblasts. However, a cosmid clone containing the entire mouse alpha 1(I) gene, including 3.7 kb of 5'- and 4 kb of 3'-flanking DNA, was expressed at reduced levels in fibroblasts overexpressing oncogenic ras. We conclude that oncogenic ras regulates the type I collagen genes at both transcriptional and posttranscriptional levels and that this effect, at least for the alpha 1(I) gene, may be mediated by sequences located either within the body of the gene itself or in the distal 3'-flanking region.

scholarly journals Regulation of collagen I gene expression by ras.

1992 ◽  
Vol 12 (10) ◽  
pp. 4714-4723 ◽  
Author(s):  
J L Slack ◽  
M I Parker ◽  
V R Robinson ◽  
P Bornstein
Keyword(s):  
Type I Collagen ◽  
The Body ◽  
Transformed Cells ◽  
Type I ◽  
Mrna Levels ◽  
Oncogenic Ras ◽  
Genes Encoding ◽  
Flanking Region ◽  
Collagen Genes ◽  
I Gene

Although transformation of rodent fibroblasts can lead to dramatic changes in expression of extracellular matrix genes, the molecular basis and physiological significance of these changes remain poorly understood. In this study, we have investigated the mechanism(s) by which ras affects expression of the genes encoding type I collagen. Levels of both alpha 1(I) and alpha 2(I) collagen mRNAs were markedly reduced in Rat 1 fibroblasts overexpressing either the N-rasLys-61 or the Ha-rasVal-12 oncogene. In fibroblasts conditionally transformed with N-rasLys-61, alpha 1(I) transcript levels began to decline within 8 h of ras induction and reached 1 to 5% of control levels after 96 h. In contrast, overexpression of normal ras p21 had no effect on alpha 1(I) or alpha 2(I) mRNA levels. Nuclear run-on experiments demonstrated that the transcription rates of both the alpha 1(I) and alpha 2(I) genes were significantly reduced in ras-transformed cells compared with those in parental cells. In addition, the alpha 1(I) transcript was less stable in transformed cells. Chimeric plasmids containing up to 3.6 kb of alpha 1(I) 5'-flanking DNA and up to 2.3 kb of the 3'-flanking region were expressed at equivalent levels in both normal and ras-transformed fibroblasts. However, a cosmid clone containing the entire mouse alpha 1(I) gene, including 3.7 kb of 5'- and 4 kb of 3'-flanking DNA, was expressed at reduced levels in fibroblasts overexpressing oncogenic ras. We conclude that oncogenic ras regulates the type I collagen genes at both transcriptional and posttranscriptional levels and that this effect, at least for the alpha 1(I) gene, may be mediated by sequences located either within the body of the gene itself or in the distal 3'-flanking region.

scholarly journals Immunohistochemistry of Parasitic Subepidermal Vesiculobullous Disease in American Badgers (Taxidea Taxus)

1994 ◽  
Vol 6 (1) ◽  
pp. 72-76 ◽  
Author(s):  
Donal O'Toole ◽  
Val Welch ◽  
Beth Williams
Keyword(s):  
Basement Membrane ◽  
Collagen Iv ◽  
Positive Staining ◽  
Taxidea Taxus ◽  
Human Collagen ◽  
Vascular Channels ◽  
Proximal Thigh ◽  
Membrane Components ◽  
Free Ranging ◽  
Basement Membrane Components

Some populations of free-ranging American badgers (Taxidea taxus) develop a distinctive seasonal dermatitis due to the subcutaneous filariid Filaria taxideae. Subepidermal vesicles that contain filarial ova develop in thinly haired skin of the inguinal area, proximal thigh, and ventral abdomen. The purpose of this study was to establish by immunohistochemistry whether basement membrane components colocalized with the roof or floor of vesicles and to confirm that filarial ova occur in intradermal vessels. Samples of skin with characteristic F. taxideae-induced subepidermal vesicles were collected from 10 adult male (n = 8) and female (n = 2) badgers. Samples were fixed in formalin for 1–4 days and processed routinely into paraffin wax. Immunohistochemical staining for basement membrane was attempted with anti-collagen IV antibodies (AM168-5M, AR079-5R, AB748) and antilaminin antibodies (MA078-5C, AR078-5R, L-9393). Optimal results in skin from badgers were obtained using a biotin-streptavidin technique and AR079-5R (anti-human collagen IV) and AR078-5R (anti-murine laminin). There was positive staining of the floor of vesicles in 5 of 6 badgers tested with antibodies to laminin and collagen IV. In 5/10 badgers, filarial ova and first stage F. taxideae larvae were found in dilated vascular channels of the upper dermis, and these vessels stained positively for factor VIII-related antigen. The results suggest that F. taxideae-induced subepidermal separation occurs consistently in the lamina lucida portion of the basal lamina and that filarial ova occur in dermal vessels.

scholarly journals High recombination between two physically close human basement membrane collagen genes at the distal end of chromosome 13q.

1988 ◽  
Vol 85 (8) ◽  
pp. 2701-2705 ◽  
Author(s):  
A. M. Bowcock ◽  
J. M. Hebert ◽  
E. Wijsman ◽  
I. Gadi ◽  
L. L. Cavalli-Sforza ◽  
...  
Keyword(s):  
Basement Membrane ◽  
Basement Membrane Collagen ◽  
Collagen Genes ◽  
Chromosome 13Q ◽  
Membrane Collagen

scholarly journals CLINICAL CASES OF BULLOUS EPIDERMOLYSIS IN NEWBORNS

2020 ◽  
Vol 10 (4(38)) ◽  
pp. 87-91
Author(s):  
O. Rubina ◽  
K. Bertsun ◽  
O. Izyumetsʹ ◽  
R. Gomon ◽  
A. Zadorozhna
Keyword(s):  
Basement Membrane ◽  
Malignant Tumors ◽  
Clinical Manifestations ◽  
Multidisciplinary Care ◽  
Basal Membrane ◽  
Dna Diagnosis ◽  
Optimal Care ◽  
Mucous Membranes ◽  
Genes Encoding ◽  
Clinical Cases

Summary. Hereditary bullous epidermolysis (BE) is a group of genetically and clinically heterogeneous diseases characterized by the formation of blisters and erosion due to injury on the skin and mucous membranes. Different forms of BE can be accompanied by various extracutaneous complications, such as blisters and erosion on the cornea and mucous membranes, stenoses and strictures of the respiratory system, gastrointestinal tract, urinary system, muscular dystrophy, and malignant tumors. Hereditary bullous epidermolysis is divided into three types, depending on the level of blister formation: simple, borderline, and dystrophic. Simple BE is characterized by the stratification of epidermis due to the keratinocyte cytolysis.  Borderline BE means that blisters are formed at the border of the epidermis and dermis due to the splitting of the lamina of the basement membrane (lamina lucida), while dystrophic BE has blisters that are formed under the dense plate of the basement membrane (lamina densa), which exfoliates the dermis. Currently, mutations have been identified in more than 10 genes encoding the structural proteins of keratinocytes and the basal membrane of the skin and mucous membranes. A common feature of these proteins is their involvement in the formation of strong bonds between the epithelium and the basement membrane. The nature of the mutations and their localization determine the severity of the clinical manifestations of BE. Mutation information is a prerequisite for effective medical and genetic counseling, prenatal and preimplantation DNA diagnosis. Therefore diagnosis and prescribing appropriate treatment and follow-up care is an important task for neonatologists and pediatric dermatologists. As manifestations of hereditary BE are numerous, a specialized center is required for optimal care, where multidisciplinary care will be provided (neonatologists, pediatric surgeons, pediatric dermatologists, etc.). The purpose of clinical observation is to pay attention of specialists to this rare disease, and to present 2 clinical cases of bullous epidermolysis in newborns who were admitted to the anesthesiology and intensive care unit of newborns of Vinnytsia Regional Children's Clinical Hospital almost at the same time.

Gene Structure: Cartilage and Basement Membrane Collagen Genes

1985 ◽  
Vol 460 (1 Biology, Chem) ◽  
pp. 524-526
Author(s):  
YOSHIHIKO YAMADA ◽  
KIMITOSHI KOHNO ◽  
YOSHIKI SAKURAI ◽  
PILAR FERNANDEZ ◽  
ANNE MARIE NUNEZ ◽  
...  
Keyword(s):  
Basement Membrane ◽  
Gene Structure ◽  
Basement Membrane Collagen ◽  
Collagen Genes ◽  
Membrane Collagen

Normal and Mutant Human Collagen Genes

1985 ◽  
Vol 460 (1 Biology, Chem) ◽  
pp. 461-462 ◽  
Author(s):  
R. KAUFMAN ◽  
E. HENKE ◽  
M. DUVIC ◽  
F. BISAT ◽  
S. PINNELL
Keyword(s):  
Human Collagen ◽  
Collagen Genes
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