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Related Concept Videos

Mitochondrial Membranes01:45

Mitochondrial Membranes

11.7K
A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
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The Inner Mitochondrial Membrane01:28

The Inner Mitochondrial Membrane

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The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria.  In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
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Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

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Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
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Structure of Porins01:21

Structure of Porins

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Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
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Related Experiment Video

Updated: May 1, 2026

Mitochondrial Ca2+ Retention Capacity Assay and Ca2+-triggered Mitochondrial Swelling Assay
05:53

Mitochondrial Ca2+ Retention Capacity Assay and Ca2+-triggered Mitochondrial Swelling Assay

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Ultrastructural studies on mitochondrial swelling.

W H Butler, J D Judah

    The Biochemical Journal
    |August 1, 1970
    PubMed
    Summary
    This summary is machine-generated.

    Valinomycin causes rapid mitochondrial swelling, while calcium and phosphate induce slower swelling. Repeated swelling and contraction cycles lead to matrix material loss, indicating irreversible mitochondrial damage.

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    Area of Science:

    • Mitochondrial physiology and structure
    • Cellular response to ionophores and inorganic phosphate

    Background:

    • Mitochondria are crucial for cellular energy production.
    • Mitochondrial morphology is sensitive to ionic and osmotic conditions.

    Purpose of the Study:

    • To investigate the effects of valinomycin, calcium chloride, and inorganic phosphate on mitochondrial structure.
    • To analyze the reversibility of mitochondrial swelling induced by these agents.

    Main Methods:

    • Mitochondria were fixed using potassium permanganate in suspension.
    • Mitochondrial morphology changes were observed after treatment with valinomycin, calcium chloride, and inorganic phosphate.

    Main Results:

    • Valinomycin induced rapid potassium influx and mitochondrial swelling with matrix space expansion and cristae out-folding.
    • Swelling induced by valinomycin was partially reversible, with incomplete cristae reformation and a blebbed appearance.
    • Repeated swelling-contraction cycles resulted in progressive loss of matrix material.
    • Calcium chloride and inorganic phosphate caused slow mitochondrial swelling.
    • ATP-induced shrinkage was incomplete and did not restore original mitochondrial structure.

    Conclusions:

    • Valinomycin, calcium, and inorganic phosphate induce distinct patterns of mitochondrial swelling.
    • Mitochondrial structure is compromised by repeated swelling and contraction cycles.
    • ATP-mediated shrinkage does not fully reverse induced mitochondrial structural changes.