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Related Concept Videos

The Bone Matrix01:18

The Bone Matrix

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Bone contains a relatively small number of cells entrenched in a matrix of collagen fibers that provide an adherent surface for inorganic salt crystals. Both components of the matrix, organic and inorganic, contribute to the unusual properties of bone. Without collagen, bones would be brittle and shatter easily. Without mineral crystals, bones would flex and provide little support. This can be observed by an experiment: when the minerals of a bone are dissolved by soaking the bone in...
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Collagens are the Major Structural Proteins of ECM01:13

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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.
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Fibril-associated Collagen01:11

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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.
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Bone Remodeling01:40

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Bone remodeling is a continuous and balanced process of bone resorption by osteoclasts and bone formation by osteoblasts. In adults, it helps maintain bone mass and calcium homeostasis. While mechanical stress can stimulate turnover as part of the normal maintenance and reparative process, several hormones also regulate bone remodeling.
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Bone Disorders01:29

Bone Disorders

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Aging and its effect on bone remodeling is the most common cause of bone disorders. In young and healthy people, bone deposition and resorption happen at an equal rate to maintain optimal bone health.
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Type IV Collagen of Basal Lamina01:05

Type IV Collagen of Basal Lamina

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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...
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Related Experiment Video

Updated: Nov 19, 2025

Enrichment of Extracellular Matrix Proteins from Tissues and Digestion into Peptides for Mass Spectrometry Analysis
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Enrichment of Extracellular Matrix Proteins from Tissues and Digestion into Peptides for Mass Spectrometry Analysis

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Proteome Variation with Collagen Yield in Ancient Bone.

Noemi Procopio1,2, Rachel J A Hopkins3,4, Virginia L Harvey2,5

  • 1Forensic Science Research Group, Faculty of Health and Life Sciences, Northumbria University, Northumbria University Newcastle, Ellison Building, Newcastle Upon Tyne NE1 8ST, U.K.

Journal of Proteome Research
|February 2, 2021
PubMed
Summary
This summary is machine-generated.

Ancient bone samples with low "collagen yield" still contain valuable proteins. Proteomic analysis of discarded bone fractions reveals informative noncollagenous proteins, useful for species identification and phylogenetic studies.

Keywords:
NCPsancient bonecollagenproteomicsradiocarbon datingstable isotopes

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Area of Science:

  • Archaeometry
  • Paleoproteomics
  • Biogeochemistry

Background:

  • Isotope analyses of ancient bone are crucial for diet and chronology.
  • Collagen yield is a routine proxy for bone preservation, with low yields (<1%) often discarded for radiocarbon dating.
  • The protein content of low-yield samples is typically underestimated.

Purpose of the Study:

  • To investigate the endogeneity and variability of proteins in discarded bone fractions using proteomic methods.
  • To correlate protein content with the "collagen yield" proxy.
  • To assess the potential of these fractions for molecular analyses.

Main Methods:

  • Proteomic analysis using MALDI-TOF and LC-ESI-MS/MS on 29 archaeological bone samples.
  • Evaluation of acid-soluble fractions typically discarded during radiocarbon dating.
  • Correlation of proteomic data with "collagen yield" measurements.

Main Results:

  • Discarded bone fractions contain significant amounts of collagenous and noncollagenous proteins (NCPs).
  • Protein abundance in these fractions did not correlate with "collagen yield".
  • Extracted NCPs were comparable to those from well-preserved samples and useful for species identification and phylogenetic studies.

Conclusions:

  • Low "collagen yield" in ancient bone does not necessarily indicate a lack of protein.
  • Discarded bone fractions can yield valuable molecular sequence-based information.
  • Retaining and analyzing these waste fractions enhances the utility of archaeological samples for diverse analyses.