Use of integrins to date the endometrium
B A Lessey1, A J Castelbaum, L Wolf
1University of North Carolina, Chapel Hill, North Carolina, USA. lessey@med.unc.edu
Fertility and Sterility
|March 25, 2000
Summary
Endometrial dating using integrin expression shows high accuracy in early phases but less agreement in later phases compared to traditional histology. Integrin expression is linked to infertility factors like endometriosis.
Area of Science:
- Reproductive endocrinology and infertility research.
- Gynecologic pathology and diagnostics.
Background:
- Accurate endometrial dating is crucial for assessing reproductive health.
- Traditional histologic dating has been the standard for decades.
- Integrin expression is a potential marker for endometrial function.
Purpose of the Study:
- To compare traditional endometrial dating with immunohistochemical integrin expression.
- To evaluate integrin expression as a diagnostic tool for endometrial receptivity.
Main Methods:
- Prospective clinical study involving 1,501 endometrial specimens.
- Immunohistochemical staining for three integrins (HSCORE) compared to histologic dating.
- Analysis of patient data including infertility factors and cycle timing.
Main Results:
- High concordance (95%, 85%) between integrin staining and histology in proliferative/early secretory phases.
- Lower concordance (54%, 49%) in mid/late secretory phases, with most disagreement in the midluteal phase.
- Absent beta3 integrin subunit expression correlated with endometriosis and male factor infertility.
Conclusions:
- Traditional histologic endometrial dating remains the gold standard.
- Integrin markers offer additional insights into endometrial function but do not replace current methods.
- Further research may refine the role of integrins in assessing endometrial receptivity.
Related Concept Videos
01:10Integrins
Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
01:15Activation of Integrins
Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
01:17Intracellular Signaling Affects Focal Adhesions
Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Some...