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Related Concept Videos

Determination01:51

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 Function01:56

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...
Growth of Cartilage and Bone Tissue01:27

Growth of Cartilage and Bone Tissue

Chondrocytes form a temporary cartilaginous model by dividing and secreting a thick gel-like extracellular matrix. Once the chondrocytes undergo programmed cell death, osteoblasts enter the site of the cartilaginous model. The process of replacing the temporary cartilaginous model with bone in an ordered manner is called endochondral ossification. In endochondral ossification, not all of the cartilage is replaced by bone tissue. Some cartilage that performs a protective and supportive function...
Collagens are the Major Structural Proteins of ECM01:13

Collagens are the Major Structural Proteins of ECM

Three main types of fibers are secreted by fibroblasts: collagen fibers, elastic fibers, and reticular fibers. Collagen fiber is made from fibrous protein subunits linked together to form a long, straight fiber. Collagen fibers, while flexible, have great tensile strength, resist stretching, and give ligaments and tendons their characteristic resilience and strength. These fibers hold connective tissues together, even during the body's movement.
Connective tissue proper includes loose...
Fibril-associated Collagen01:11

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...
Type IV Collagen of Basal Lamina01:05

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.
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Related Experiment Video

Updated: Jul 16, 2026

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
07:54

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen

Published on: September 20, 2012

Localization of type II collagen, long form alpha 1(IX) collagen, and short form alpha 1(IX) collagen transcripts in

R E Swiderski1, M Solursh

  • 1Department of Biology, University of Iowa, Iowa City 52242.

Developmental Dynamics : an Official Publication of the American Association of Anatomists
|June 1, 1992
PubMed
Summary

Avian type II and type IX collagen gene expression differs between developing cartilage and the notochord. This study reveals distinct spatial and temporal patterns of these crucial collagen transcripts during embryonic development.

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Last Updated: Jul 16, 2026

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Area of Science:

  • Developmental Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Type II collagen is a major structural component of cartilage.
  • Type IX collagen, existing in long and short forms, also plays a role in cartilage matrix organization.
  • Understanding the differential expression of these collagens is key to deciphering skeletal development.

Purpose of the Study:

  • To compare the spatial and temporal expression of avian type II collagen and type IX collagen (long and short forms) transcripts.
  • To investigate the expression patterns during notochord and axial skeleton development.
  • To elucidate the regulatory pathways of cartilage marker gene expression in different embryonic tissues.

Main Methods:

  • In situ hybridization was employed to detect and localize specific RNA transcripts.
  • Analysis focused on the developing avian notochord, axial skeleton, chondrocranium, and Meckel's cartilage.
  • Expression patterns were examined across developmental stages (specifically stages 25-28).

Main Results:

  • Type II collagen and short form type IX collagen transcripts were found in the developing nonchondrogenic notochord.
  • Long form type IX collagen transcripts were absent in the notochord and perinotochordal sheath.
  • All three transcripts (type II collagen, long and short type IX collagen) were co-localized in developing chondrogenic tissues like vertebrae, chondrocranium, and Meckel's cartilage.
  • Short form type IX collagen expression was more restricted than the long form in chondrogenic regions.

Conclusions:

  • The study highlights differential expression of type II and type IX collagen transcripts in chondrogenic versus nonchondrogenic tissues during avian embryogenesis.
  • Findings suggest a complex regulatory mechanism governing cartilage marker gene expression.
  • This research provides further evidence for distinct roles of collagen isoforms in skeletal development.