Related Experiment Video
Updated: Jun 30, 2026

12:23
Granulocyte-dependent Autoantibody-induced Skin Blistering
Published on: October 12, 2012
Developmental regulation of collagen differential expression in the rabbit bladder
1Division of Pediatric Urology, Children's Hospital and Medical Center, University of Washington, Seattle, USA.
The Journal of Urology
|August 1, 1996
Summary
Collagen types I and III gene expression is developmentally regulated in rabbit bladders. Their complex regulation during early growth impacts bladder extracellular matrix development and may influence injury response.
Area of Science:
- Urology
- Developmental Biology
- Biochemistry
Background:
- Bladder compliance is influenced by collagen composition.
- Understanding collagen synthesis and degradation is crucial for bladder development.
Purpose of the Study:
- Investigate collagen types I and III gene expression in developing rabbit bladders.
- Characterize the relationship between collagen gene expression and bladder growth.
Main Methods:
- Utilized New Zealand white rabbits from fetal to adult stages.
- Analyzed collagen types I and III messenger RNA (mRNA) using Northern blot hybridization.
- Localized mRNA transcripts and corresponding protein distributions via in situ hybridization and immunohistochemical staining.
Main Results:
- Collagen types I and III expression is developmentally regulated at the gene expression level.
- Temporal and spatial distribution of alpha 1(I) and alpha 1(III) mRNA correlates with extracellular protein deposition.
- Differential distribution of mRNA transcripts is also developmentally regulated.
Conclusions:
- Characterized collagen gene expression during normal rabbit bladder development.
- Observed alterations in alpha 1(I) and alpha 1(III) expression as the bladder grows.
- Highlighted the complexity of the extracellular matrix in young bladders due to nonconcordant collagen mRNA regulation, potentially impacting injury response.
Related Concept Videos
Determination
During embryogenesis, cells become progressively committed to different fates through a two-step process: specification followed by determination. Specification is demonstrated by removing a segment of an early embryo, “neutrally” culturing the tissue in vitro—for example, in a petri dish with simple medium—and then observing the derivatives. If the cultured region gives rise to cell types that it would normally generate in the embryo, this means that it is specified. In contrast, determination...
Structural Protein Function
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...
Fibril-associated Collagen
Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
Type IV Collagen of Basal Lamina
Type IV collagen is a 400 nm long, network-forming collagen that acts as a barrier between the epithelial and endothelial cells. Type IV collagen forms the backbone of the basement membrane by scaffolding with laminin, entactin, proteoglycans, and fibronectin. Apart from rendering structural support to the basement membrane, it also helps entail signaling potentials necessary for both pathological and physiological functions.
A type IV collagen molecule has six alpha chains which can exist in...
A type IV collagen molecule has six alpha chains which can exist in...

